Trophic factor combinations for nervous system treatment

ABSTRACT

The present invention relates to a composition including an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect and an effective amount of a neurotrophin. The composition can also include an effective amount of at least one of a growth factor and a neuropeptide. The present invention also relates a method of treating an injury to a nervous system of an animal that includes the steps of identifying the injury to the nervous system and applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect. The method can also include applying an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide to the injury.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a divisional application of patent application Ser. No. 11/214,372, filed Aug. 29, 2005 now abandoned, which claims priority under 35 U.S.C. §119(e) to U.S. Provisional Patent Application No. 60/604,912, filed Aug. 27, 2004, the entirety of which is incorporated by reference herein.

REFERENCE TO GOVERNMENT GRANT

This invention was made with United States government support awarded by the National Institutes of Health, Grant # HL069064. The United States has certain rights in this invention.

FIELD OF THE INVENTION

The invention relates to combinations of neurochemically active agents for treating a nervous system and the methods of treating a nervous system with the combinatorial treatments.

SUBMISSION OF SEQUENCE LISTING

The contents of the electronic submission of text file Sequence Listing is incorporated herein by reference in its entirety.

BACKGROUND OF THE INVENTION

The nervous system is comprised of two divisions: the central nervous system (CNS) and the peripheral nervous system (PNS). The CNS includes the brain and the spinal cord and controls most functions of the body and mind. The remainder of the nervous system is the PNS. Nerves of the PNS connect the CNS to sensory organs (such as the eyes and ears), other organs of the body, muscles, blood vessels, and glands. The peripheral nerves include the cranial nerves, the spinal nerves, and roots.

The CNS controls all voluntary movement, such as movement of the legs during walking, and all involuntary movement, such as beating of the heart. The spinal cord connects the body and the brain by transmitting information to and from the body and the brain.

The nervous system can be injured in numerous ways, and injuries can be traumatic. For instance, sudden physical assault on a portion of the nervous system results in a traumatic injury. In the case of a traumatic brain injury, the injury can be focal, i.e., confined to a specific area of the brain, or diffuse, i.e., involving more than one area of the brain.

Injuries to the nervous system include contusions, which are bruises of the nervous system, and blood clots. Blood clots can form in or around the nervous system. For example, when bleeding occurs between the skull and the brain, the blood forms a clot. This puts pressure on the brain, which can lead to changes in brain function.

Spinal cord injuries (SCI) are a particular type of injury to the nervous system. As of the year 2000, approximately 450,000 people in the United States have sustained SCI, with more than 10,000 new cases reported in the United States every year. Motor vehicle accidents are the leading cause of SCI (44 percent), followed by acts of violence (24 percent), falls (22 percent), sports injuries (8 percent), and other causes (2 percent). Of the 10,000 new cases of SCI in the United States each year, 51.7% have tetraplegia, i.e., injuries to one of the eight cervical segments of the spinal cord, and 56.7% have paraplegia, i.e., lesions in the thoracic, lumbar, or sacral regions of the spinal cord. Since 1990, the most frequent neurologic category is incomplete tetraplegia (29.5%), followed by complete paraplegia (27.9%), incomplete paraplegia (21.3%), and complete tetraplegia (18.5%).

With spinal cord injuries in the neck, significant impairment of breathing may result. The most frequent site of spinal injury is the neck or cervical region and, of these, the major cause of death arises from respiratory complications. For patients that survive a major spinal cord injury in the neck, they may spend the rest of their lives depending on an artificial ventilator or phrenic nerve pacemaker to sustain their lives. For others with less severe respiratory impairment, they may be able to breathe normally, but are unable to sigh or breathe deeply and maintain the integrity of the lung. As a consequence, regions of the lung will collapse in these patients, causing pneumonia and allowing other respiratory infections to become established. Clearly, restoration of normal breathing ability, including deep breaths and sighs, is a major goal in the treatment of spinal cord injury patients.

Injury to the spinal cord and other parts of the nervous system may be particularly devastating to life and the quality of life. In addition, injury to the nervous system can engender serious economic losses to the individual and to society. Currently, there are few effective treatment options available for patients with spinal cord injuries, although there are a few promising indications that physical therapy or chronic intermittent hypoxia (CIH), may have beneficial effects. Exposure to intermittent hypoxic episodes has been shown to initiate spinal protein synthesis. However, studies have also shown that chronic intermittent hypoxia has other drawbacks as a treatment for spinal cord injuries. For example, certain CIH treatment methods can cause systemic hypertension, altered sympathetic chemoreflexes, and hippocampal cell death by the process of apoptosis.

Physical training and preconditioning have been used to treat SCI. Almost all patients with spinal cord injuries can now achieve a partial return of function with proper physical therapy that maintains flexibility and function of the muscles and joints, and strengthens the neural pathways that underlie movement. Physical therapy can also help reduce the risk of blood clots and boost the patient's morale. Physical training currently being investigated includes body weight-supported treadmill training, in which patients with partial spinal cord injury “walk” on a treadmill while they are partially supported through the use of a specially designed harness attached to an overhead lift. Unfortunately, this type of therapy is very expensive, and efficacy is far from complete.

SUMMARY OF THE INVENTION

The invention, which is defined by the claims set out at the end of this disclosure, is intended to solve at least some of the problems noted above. A composition is provided that includes an effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The composition also includes an effective amount of a neurotrophin.

In another embodiment, the composition also includes an effective amount of at least one of a growth factor and a neuropeptide.

Also provided is a method of treating an injury to a nervous system of an animal. In one embodiment, the method includes the steps of identifying the injury to the nervous system and applying to the injury an effective amount of at least one of antimicrobial peptide and a substance having an antimicrobial peptide effect.

In another embodiment, an injury to the nervous system is identified. An effective amount of at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect is combined with an effective amount of one or more trophic factors selected from the group consisting of a growth factor, a neurotrophin, and a neuropeptide. The combination is applied to the injury.

A kit is also provided. In an embodiment, the kit includes at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect. The kit also includes a neurotrophin. In another embodiment, the kit also includes a viscous substance. In some embodiments, the kit also includes at least one of a growth factor and a neuropeptide.

BRIEF DESCRIPTION OF THE DRAWINGS

Preferred exemplary embodiments of the invention are illustrated in the accompanying drawings in which:

FIG. 1 is a graph showing change in body weight at 2 weeks after spinal cord injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, the body weight is shown for spinal injury alone (black bar) and for spinal injury and a trophic factor combination made in accordance with the invention (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 2 is a graph showing peak neurogram voltages from the phrenic nerve during inspiration on the side of injury (Y-axis) at 2 weeks post-injury in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, neurogram voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 3 is a graph showing evoked potential voltage (in volts) from the phrenic neurogram on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). The stimulating current was 1000 uA. For each strain of rats, evoked potential voltages are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 4 is a graph showing the stimulating current (in uAmps) required to evoke potentials in the phrenic nerve on the side of injury at 2 weeks post-injury (Y-axis) in two strains of rats, Sprague Dawley and Lewis (X-axis). For each strain of rats, stimulating currents are shown for spinal injury alone (black bar) and for spinal injury and the trophic factor combination (grey bar). In addition, corresponding data are shown for all rats combined.

FIG. 5 is a graph showing the change in body mass in grams at 2 weeks post-injury (Y-axis) in different Lewis rats (X-axis). The body weight is shown for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs). FIG. 5 also shows change in phrenic amplitude at 2 weeks post-injury (Y-axis) in the rats (X-axis) for spinal injury alone (SCI) and for spinal injury and a trophic factor combination made in accordance with the invention (SCI+NTs).

Before explaining embodiments of the invention in detail, it is to be understood that the invention is not limited in its application to the details of construction and the arrangement of the components set forth in the following description or illustrated in the drawings. The invention is capable of other embodiments or being practiced or carried out in various ways. Also, it is to be understood that the phraseology and terminology employed herein is for the purpose of description and should not be regarded as limiting.

DETAILED DESCRIPTION Definitions

To facilitate understanding of the invention, a number of terms are defined below.

As used herein, the term “antimicrobial polypeptide” refers to polypeptides that inhibit the growth of microbes (e.g., bacteria). Examples of antimicrobial polypeptides include, but are not limited to, the polypeptides described in Tables 1 and 2 below. Antimicrobial polypeptides include peptides synthesized from both L-amino and D-amino acids.

As used herein, the term “pore forming agent” refers to any agent (e.g., peptide or other organic compound) that forms pores in a biological membrane. When the pore forming agent is a peptide, the peptide can be synthesized from both L-amino and D-amino acids.

As used herein, the term “growth factor” refers to any compound that is involved in cell differentiation and growth. Growth factors can be proteins (e.g., IGF-1 (insulin-like growth factor 1), IGF-2 (insulin-like growth factor 2), NGF-β (nerve growth factor-β), EGF (epidermal growth factor), CSGF (colony-stimulating growth factor), FGF (fibroblast growth factor), PDGF (platelet-derived growth factor), VEGF (vascular endothelial growth factor), TGF-β (transforming growth factor β, and bone morphogenetic proteins)), either purified from natural sources or genetically engineered, as well as fragments, mimetics, and derivatives or modifications thereof. Further examples of growth factors are provided in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.

The term “trophic factor” as used herein refers to a substance that stimulates growth and development or stimulates increased activity.

The term “hyaluronic acid” includes hyaluronic acid and its derivatives, for instance, esters, salts such as the sodium, potassium, magnesium, calcium, alkaline, alkaline earth metals, and the like, and derivatives such as sulphated or polysulphated hyaluronates, or hyaluronates that have been otherwise modified in a manner way such that the function of hyaluronic acid is retained.

The term “recombinant protein” or “recombinant polypeptide” as used herein refers to a protein molecule expressed from a recombinant DNA molecule. In contrast, the term “native protein” or “native polypeptide” is used herein to indicate a protein isolated from a naturally occurring (i.e., a nonrecombinant) source. Molecular biological techniques may be used to produce a recombinant form of a protein or polypeptide with similar or identical properties as compared to the native form of the protein.

Where an amino acid sequence is recited herein to refer to an amino acid sequence of a naturally occurring protein molecule, amino acid sequence and like terms, such as polypeptide or protein are not meant to limit the amino acid sequence to the complete, native amino acid sequence associated with the recited protein molecule.

As used herein in reference to an amino acid sequence or a protein, the term “portion” (as in “a portion of an amino acid sequence”) refers to fragments of that protein. The fragments may range in size from four amino acid residues to the entire amino acid sequence minus one amino acid (e.g., 5, 6, 7, 8, . . . x−1).

As used herein, the term “variant,” when used in reference to a protein, refers to a protein encoded by partially homologous nucleic acids so that the amino acid sequence of the protein varies. As used herein, the term “variant” encompasses proteins encoded by homologous genes having both conservative and nonconservative amino acid substitutions that do not result in a change in protein function, as well as proteins encoded by homologous genes having amino acid substitutions that cause decreased protein function or increased protein function.

As used herein, the term “fusion protein” refers to a chimeric protein containing the protein of interest (e.g., defensins and fragments thereof) joined to a heterologous protein fragment (e.g., the fusion partner which consists of a non-defensin protein). The fusion partner may enhance the solubility of a defensin as expressed in a host cell, may provide an affinity tag to allow purification of the recombinant fusion protein from the host cell or culture supernatant, or both. If desired, the fusion protein may be removed from the protein of interest (e.g., defensin or fragments thereof) by a variety of enzymatic or chemical processes known to the art.

As used herein, the term “purified” refers to molecules, either nucleic or amino acid sequences, that are removed from their natural environment, isolated, or separated. The percent of a purified component is thereby increased in the sample. For example, an isolated defensin is therefore a purified defensin. Substantially purified molecules are at least 60% free, preferably at least 75% free, and more preferably at least 90% free from other components with which they are naturally associated.

The term “gene” as used herein, refers to a DNA sequence that comprises control and coding sequences necessary for the production of a polypeptide or protein precursor. The polypeptide can be encoded by a full length coding sequence or by any portion of the coding sequence, as long as the desired protein activity is retained.

The term “homology” refers to a degree of complementarity. There may be partial homology or complete homology (i.e., identity). A “partially complementary sequence” is one that at least partially inhibits a completely complementary sequence from hybridizing to a target nucleic acid. This situation is referred to using the functional term “substantially homologous.” The inhibition of hybridization of the completely complementary sequence to the target sequence may be examined using a hybridization assay (e.g., Southern or Northern blot, solution hybridization, and the like) under conditions of low stringency. A substantially homologous sequence or probe will compete for and inhibit the binding (i.e., the hybridization) of a completely homologous sequence or probe to a target under conditions of low stringency. This is not to say that conditions of low stringency are such that non-specific binding is permitted; low stringency conditions require that the binding of two sequences to one another be a specific (i.e., selective) interaction. The absence of non-specific binding may be tested by the use of a second target that lacks even a partial degree of complementarity (e.g., less than about 30% identity). In this case, in the absence of non-specific binding, the probe will not hybridize to the second non-complementary target.

When used in reference to a double-stranded nucleic acid sequence such as a cDNA or a genomic clone, the term “substantially homologous” refers to any probe which can hybridize to either or both strands of the double-stranded nucleic acid sequence under conditions of low stringency as described herein.

As used herein, the term “hybridization” is used in reference to the pairing of complementary nucleic acid strands. Hybridization and the strength of hybridization (i.e., the strength of the association between nucleic acid strands) is impacted by many factors well known in the art including the degree of complementarity between the nucleic acids, stringency of the conditions involved affected by such conditions as the concentration of salts, the T_(m) (melting temperature) of the formed hybrid, the presence of other components (e.g., the presence or absence of polyethylene glycol), the molarity of the hybridizing strands, and the G:C content of the nucleic acid strands.

As used herein, the term “stringency” is used in reference to the conditions of temperature, ionic strength, and the presence of other compounds, under which nucleic acid hybridizations are conducted. With high stringency conditions, nucleic acid base pairing will occur only between nucleic acid fragments that have a high frequency of complementary base sequences. Thus, conditions of medium or low stringency are often required when it is desired that nucleic acids that are not completely complementary to one another be hybridized or annealed together. It is well known in the art that numerous equivalent conditions can be employed to comprise medium or low stringency conditions. The choice of hybridization conditions is generally evident to one skilled in the art and is normally guided by the purpose of the hybridization, the type of hybridization (DNA-DNA or DNA-RNA), and the level of desired relatedness between the sequences (e.g., Sambrook et al., 1989, Nucleic Acid Hybridization, A Practical Approach, IRL Press, Washington D.C., 1985, for a general discussion of the state of the art).

The stability of nucleic acid duplexes is known to decrease with an increased number of mismatched bases, and further to be decreased to a greater or lesser degree depending on the relative positions of mismatches in the hybrid duplexes. Thus, the stringency of hybridization can be used to maximize or minimize stability of such duplexes. Hybridization stringency can be altered, for example, by adjusting the temperature of hybridization; adjusting the percentage of helix destabilizing agents, such as formamide, in the hybridization mix; and adjusting the temperature and/or salt concentration of the wash solutions. For filter hybridizations, the final stringency of hybridizations can be determined by the salt concentration and/or temperature used for the post-hybridization washes.

“High stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5×Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 0.1×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

“Medium stringency conditions” when used in reference to nucleic acid hybridization comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.5% SDS, 5×Denhardt's reagent and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 1.0×SSPE, 1.0% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

“Low stringency conditions” comprise conditions equivalent to binding or hybridization at 42° C. in a solution consisting of 5×SSPE (43.8 g/l NaCl, 6.9 g/l NaH₂PO₄.H₂O and 1.85 g/l EDTA, pH adjusted to 7.4 with NaOH), 0.1% SDS, 5×Denhardt's reagent [50×Denhardt's contains per 500 ml: 5 g Ficoll (Type 400, Pharamcia), 5 g BSA (Fraction V; Sigma)] and 100 μg/ml denatured salmon sperm DNA followed by washing in a solution comprising 5×SSPE, 0.1% SDS at 42° C. when a probe of about 500 nucleotides in length is employed.

As used herein, the term “T_(m)” is used in reference to the melting temperature, which is the temperature at which 50% of a population of double-stranded nucleic acid molecules becomes dissociated into single strands. The equation for calculating the Tm of nucleic acids is well known in the art. The T_(m) of a hybrid nucleic acid can be estimated using a formula adopted from hybridization assays in 1 M salt, and commonly used for calculating T_(m) for PCR primers: [(number of A+T)×2° C.+(number of G+C)×4° C.]. (C. R. Newton et al., PCR, 2nd Ed., Springer-Verlag (New York, 1997), p. 24). This formula was found to be inaccurate for primers longer than 20 nucleotides. (Id.) Another simple estimate of the T_(m) value can be calculated by the equation: T_(m)=81.5+0.41(% G+C), when a nucleic acid is in aqueous solution at 1 M NaCl. (e.g., Anderson and Young, Quantitative Filter Hybridization, in Nucleic Acid Hybridization (1985). Other more sophisticated computations exist in the art which take structural as well as sequence characteristics into account for the calculation of T_(m). A calculated T_(m) is merely an estimate; the optimum temperature is commonly determined empirically.

As used herein, the term “vector” is used in reference to nucleic acid molecules that transfer DNA segment(s) from one cell to another and capable of replication in a cell. Vectors may include plasmids, bacteriophages, viruses, cosmids, and the like.

The terms “recombinant vector” and “expression vector” as used herein refer to DNA or RNA sequences containing a desired coding sequence and appropriate DNA or RNA sequences necessary for the expression of the operably linked coding sequence in a particular host organism. Prokaryotic expression vectors include a promoter, a ribosome binding site, an origin of replication for autonomous replication in host cells and can also include other sequences, e.g., an optional operator sequence. A “promoter” is defined as a DNA sequence that directs RNA polymerase to bind to DNA and to initiate RNA synthesis. Eukaryotic expression vectors include a promoter, polyadenlyation signal and optionally an enhancer sequence.

As used herein the term “coding region” when used in reference to structural gene refers to the nucleotide sequences which encode the amino acids found in the nascent polypeptide as a result of translation of a mRNA molecule. Typically, the coding region is bounded on the 5′ side by the nucleotide triplet ATG, which encodes the initiator methionine, and on the 3′ side by a stop codon (e.g., TAA, TAG, TGA). In some cases, the coding region is also known to initiate by a nucleotide triplet TTG.

The terms “buffer” or “buffering agents” refer to materials that when added to a solution, cause the solution to resist changes in pH.

The term “monovalent salt” refers to any salt in which the metal (e.g., Na, K, or Li) has a net 1+ charge in solution (i.e., one more proton than electron).

The term “divalent salt” refers to any salt in which a metal (e.g., Mg, Ca, or Sr) has a net 2+ charge in solution.

The term “solution” refers to an aqueous mixture.

The term “buffering solution” refers to a solution containing a buffering reagent.

The present invention relates to neurochemically active agents and combinations thereof. Neurochemically active agents include one or more antimicrobial peptide and/or a substance having an antimicrobial peptide effect. Antimicrobial peptides themselves are known to have trophic effects. As such, an antimicrobial peptide and/or a substance having an antimicrobial peptide effect can be used by itself in the methods of the invention. Neurochemically active agents also include one or more growth factor, neurotrophin, and neuropeptide. Combinations of neurochemically active agents are referred to herein as “trophic factor combinations.”

According to the invention, neurochemically active agents can be used alone or in combination to treat injuries to the nervous system, i.e., the central nervous system and the peripheral nervous system. The one or more neurochemically active agents can be used to treat nervous system injuries, including trauma induced injuries, degenerative induced injuries, age induced injuries, and infection induced injuries. Injuries that can be treated include, but are not limited to, spinal cord injury, including severed spinal cords; peripheral nerve damage, brain injuries, e.g., blood clots, tumors, strokes, and ischemis and perfusion; and Parkinson's disease, Alzheimer disease, muscular dystrophy, amyotrophic lateral sclerosis, multiple sclerosis, Pick's disease, prion diseases, Huntington disease, and related disorders.

When applied to a the nervous system, trophic factor combinations of the invention result in at least one of the following: lower loss in body weight after the injury when compared to controls not receiving the trophic factor combinations, strengthened motor recovery in injured animals treated with the trophic factor combination when compared to animals not treated with the trophic factor combination, larger evoked potentials in nerves when compared to controls not receiving the trophic factor combination, and a lower current required to evoke a response (threshold current) when compared to controls not receiving the trophic factor combination.

It is contemplated that the trophic factor combinations of the present invention used to treat injuries of the nervous system result in reduced inflammation, growth of new cells, increased plasticity, among other beneficial effects.

I. Trophic Factor Combinations

The present invention contemplates the use of trophic factor combinations and their individual components for treatment of injuries to the nervous system. Trophic factor combinations according to the invention can include one or more of the following elements: antimicrobial polypeptides (e.g., defensins), a substance having an effect of an antimicrobial peptide, a growth factor, a neurotrophin, and a neuropeptide. Additional components can also be included and are discussed below.

A. Antimicrobial Peptides

In some embodiments, one or more antimicrobial polypeptides and/or one or more substances having an antimicrobial peptide effect are used as a trophic factor to treat an injury to a nervous system. For additional information on antimicrobial peptides, see, for example, Antimicrobial Peptide Protocols, ed. W. M. Shafer, Humana Press, Totowa, N.J., 1997; and databases including http://aps.unmc.edu/AP/main.php (discussed in Wang Z, Wang G., APD: the Antimicrobial Peptide Database, Nucleic Acids Res. 2004 Jan. 1; 32(Database issue):D590-2), http://sdmc.lit.org.sg/Templar/DB/Antimic/, and http://www.bbcm.units.it/˜zelezetsk/hdpdb.html (database of defense peptides) and Table 1 below.

In some embodiments, the antimicrobial peptide is a compound or peptide selected from the following: bovine defensin peptide (BNP-1, Romeo et al., J. Biol. Chem. 263(15):9573-9575 [1988]), magainin (e.g., magainin I, magainin II, xenopsin, xenopsin precursor fragment, caerulein precursor fragment), magainin I and II analogs (PGLa, magainin A, magainin G, pexiganin, Z-12, pexigainin acetate, D35, MSI-78A, MG0 [K10E, K11E, F12W-magainin 2], MG2+ [KIOE, F12W-magainin-2], MG4+ [F12W-magainin 2], MG6+ [f12W, E19Q-magainin 2 amide], MSI-238, reversed magainin II analogs [e.g., 53D, 87-ISM, and A87-ISM], Ala-magainin II amide, magainin II amide), cecropin P1, cecropin A, cecropin B, indolicidin, nisin, ranalexin, lactoferricin B, poly-L-lysine, cecropin A (1-8)-magainin II (1-12), cecropin A (1-8)-melittin (1-12), CA(1-13)-MA(1-13), CA(1-13)-ME(1-13), gramicidin, gramicidin A, gramicidin D, gramicidin S, alamethicin, protegrin, histatin, dermaseptin, lentivirus amphipathic peptide or analog, parasin I, lycotoxin I or II, globomycin, gramicidin S, surfactin, ralinomycin, valinomycin, polymyxin B, PM2 [(+/−) 1-(4-aminobutyl)-6-benzylindane], PM2c [(+/−)-6-benzyl-1-(3-carboxypropyl)indane], PM3 [(+/−) 1-benzyl-6-(4-aminobutyl)indane], tachyplesin, buforin I or II, misgurin, melittin, PR-39, PR-26, 9-phenylnonylamine, (KLAKKLA)n, (KLAKLAK)n, where n=1, 2, or 3, (KALKALK)₃, KLGKKLG)n, and KAAKKAA)n, wherein N=1, 2, or 3, paradaxin, Bac 5, Bac 7, ceratoxin, mdelin 1 and 5, bombin-like peptides, PGQ, cathelicidin, HD-5, Oabac5alpha, ChBac5, SMAP-29, Bac7.5, lactoferrin, granulysin, thionin, hevein and knottin-like peptides, MPG1, 1bAMP, snakin, lipid transfer proteins, and plant defensins. Exemplary sequences for the above listed compounds are provided in Table 1. In some embodiments, the antimicrobial peptides or substances having an antimicrobial peptide effect (where they are peptides) are synthesized from L-amino acids, while in other embodiments, the peptides are synthesized from or comprise D-amino acids.

The compounds listed above can be isolated and purified from natural sources as appropriate. The compounds can also be produced recombinantly or synthetically, as described below.

In preferred embodiments, the trophic factor combinations of the present invention comprise one or more antimicrobial polypeptides and/or one or more substance having an antimicrobial peptide effect at a concentration of about 0.01 to about 1000 mg/L. In preferred embodiments, the trophic factor combinations comprise a solution comprising one or more antimicrobial polypeptides at a concentration of about 0.1 to about 5 mg/L.

In some embodiments of the present invention, the antimicrobial polypeptide is a defensin. In preferred embodiments, the trophic factor combinations of the present invention comprise one or more defensins. In further preferred embodiments, the trophic factor combination comprises a solution comprising purified defensins at a concentration of about 0.01 to 1000 mg/L. In particularly preferred embodiments, the trophic factor combinations comprise a solution comprising defensins at a concentration of about 0.1 to 5 mg/L. In still further preferred embodiments, the antimicrobial polypeptide is BNP1 (also known as bactanecin and bovine dodecapeptide). In certain embodiments, the defensin comprises the following consensus sequence: X₁CN₁CRN₂CN₃ERN₄CN₅GN₆CCX₂, wherein N and X represent conservatively or nonconservatively substituted amino acids and N₁=1, N₂=3 or 4, N₃=3 or 4, N₄=1, 2, or 3, N₆=5-9, X₁ and X₂ may be present, absent, or equal from 1-2.

The present invention is not limited to any particular defensin. Indeed, trophic factor combinations comprising a variety of defensins are contemplated. Representative defensins are provided in Tables 1 and 2 below. In general, defensins are a family of highly cross-linked, structurally homologous antimicrobial peptides that can be found in the azurophil granules of polymorphonuclear leukocytes (PMNs) with homologous peptides being present in macrophages (e.g., Selsted et al., Infect. Immun. 45:150-154 [1984]). Originally described as “Lysosomal Cationic Peptides” in rabbit and guinea pig PMN (Zeya et al., Science 154:1049-1051 [1966]; Zeya et al., J. Exp. Med. 127:927-941 [1968]; Zeya et al., Lab. Invest. 24:229-236 [1971]; Selsted et al., [1984], supra.), this mixture was found to account for most of the microbicidal activity of the crude rabbit PMN extract against various microorganisms (Zeya et al., [1966], supra; Lehrer et al., J. Infect. Dis. 136:96-99 [1977]; Lehrer et al., Infect. Immun. 11:1226-1234 [1975]). Six rabbit neutrophil defensins have been individually purified and are designated NP-1, NP-2, NP-3A, NP-3B, NP-4, and NP-5. Their amino acid sequences were determined, and their broad spectra of activity were demonstrated against a number of bacteria (Selsted et al., Infect. Immun. 45:150-154 [1984]), viruses (Lehrer et al., J. Virol. 54:467 [1985]), and fungi (Selsted et al., Infect. Immun. 49:202-206 [1985]; Segal et al., 151:890-894 [1985]). Defensins have also been shown to possess mitogenic activity (e.g., Murphy et al., J. Cell. Physiol. 155:408-13 [1993]).

Four peptides of the defensin family have been isolated from human PMN's and are designated HNP-1, HNP-2, HNP-3, and LNP-4 (Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]; Wilde et al., J. Biol. Chem. 264:11200-11203 [1989]). The amino acid sequences of HNP-1, HNP-2, and HNP-3 differ from each other only in their amino terminal residues, while each of the human defensins are identical to the six rabbit peptides in 10 or 11 of their 29 to 30 residues. These are the same 10 or 11 residues that are shared by all six rabbit peptides. Human defensin peptides have been shown to share with the rabbit defensins a broad spectrum of antimicrobial activity against bacteria, fungi, and enveloped viruses (Ganz et al., [1985], supra).

Three defensins designated RatNP-1, RatNP-2, and RatNP-4, have been isolated from rat (Eisenhauer et al., Infection and Immunity 57:2021-2027 [1989]). A guinea pig defensin (GPNP) has also been isolated, purified, sequenced and its broad spectrum antimicrobial properties verified (Selsted et al., Infect. Immun. 55:2281-2286 [1987]). Eight of its 31 residues were among those invariant in six rabbit and three human defensin peptides. The sequence of GPNP also included three nonconservative substitutions in positions otherwise invariant in the human and rabbit peptides. Of the defensins tested in a quantitative assay HNP-1, RatNP-1, and rabbit NP-1 possess the most potent antimicrobial properties, while NP-5 possesses the least amount of antimicrobial activity when tested against a panel of organisms in stationary growth phase (Selsted et al., Infect. Immun. 45:150-154 [1984]; Ganz et al., J. Clin. Invest. 76:1427-1435 [1985]). Defensin peptides are further described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777 (each of which is incorporated herein by reference).

Defensin peptides suitable for use alone in the methods and/or in trophic factor combinations of the present invention include natural defensin peptides isolated from known cellular sources, synthetic peptides produced by solid phase or recombinant DNA techniques, and defensin analogs which may be smaller peptides or other molecules having similar binding and biological activity as the natural defensin peptides (e.g., peptide mimetics). Methods for the purification of defensin peptides are described in U.S. Pat. Nos. 4,543,252; 4,659,692; and 4,705,777, the disclosures of which are incorporated herein by reference.

In preferred embodiments, suitable synthetic peptides will comprise all or part of the amino acid sequence of a known peptide, more preferably incorporating at least some of the conserved regions identified in Table 2. In particularly preferred embodiments, the synthetic peptides incorporate at least one of the conserved regions, more typically incorporating two of the conserved regions, preferably conserving at least three of the conserved regions, and more preferably conserving four or more of the conserved regions. In preferred embodiments, the synthetic peptides comprise fifty amino acids or fewer, although there may be advantages in increasing the size of the peptide above that of the natural peptides in certain instances. In certain embodiments, the peptides have a length in the range from about 10 to 50 amino acids, preferably being in the range from about 10 to 40 amino acids, and most preferably being in the range from about 30 to 35 amino acids which corresponds generally to the length of the natural defensin peptides.

In some cases, it may be desirable to incorporate one or more non-natural amino acids in the synthetic defensin peptides of the present invention. In preferred embodiments, non-natural amino acids comprise at least an N-terminus and a C-terminus of the peptide and have side chains that are either identical to or chemically modified or substituted from a natural amino acid counterpart. An example of a non-natural amino acid is an optical isomer of a naturally-occurring L-amino acid, such as a peptide containing all D-amino acids. Examples of the synthesis of peptides containing all D-amino acids include Merrifield et al., Ciba Found Symp. 186:5-26 (1994); Wade et al., Proc. Natl. Acad. Sci. USA 87(12):4761-5 (1990); and U.S. Pat. No. 5,792,831, which is herein incorporated by reference. Examples of chemical modifications or substitutions include hydroxylation or fluorination of C—H bonds within natural amino acids. Such techniques are used in the manufacture of drug analogs of biological compounds and are known to one of ordinary skill in the art.

Synthetic peptides having biological and binding activity the same or similar to that of natural defensin peptides can be produced by either of two exemplary approaches. First, the polypeptides can be produced by the well-known Merrifield solid-phase chemical synthesis method wherein amino acids are sequentially added to a growing chain (Merrifield, J. Am. Chem. Soc. 85:2149-2156 [1963]). Automatic peptide synthesis equipment is available from several commercial suppliers, including PE Biosystems, Inc., Foster City, Calif.; Beckman Instruments, Inc., Waldwick, N.J.; and Biosearch, Inc., San Raphael, Calif. Using such automatic synthesizers according to manufacturer's instructions, peptides can be produced in gram quantities for use in the present invention.

Second, the synthetic defensin peptides of the present invention can be synthesized by recombinant techniques involving the expression in cultured cells of recombinant DNA molecules encoding a gene for a desired portion of a natural or analog defensin molecule. The gene encoding the defensin peptide can itself be natural or synthetic. Conveniently, polynucleotides can be synthesized by well-known techniques based on the desired amino acid sequence. For example, short single-stranded DNA fragments can be prepared by the phosphoramidite method (Beaucage et al., Tetra. Lett. 22:1859-1862 [1981]). A double-stranded fragment can then be obtained either by synthesizing the complementary strand and annealing the strands together under appropriate conditions, or by adding the complementary strand using DNA polymerase under appropriate conditions, or by adding the complementary strand using DNA polymerase with an appropriate primer sequence. The natural or synthetic DNA fragments coding for the desired defensin peptide can then be incorporated in a suitable DNA construct capable of introduction to and expression in an in vitro cell culture. The DNA fragments can be portions or variants of wild-type nucleic acids encoding defensins. Suitable variants include those both with conservative and nonconservative amino acid substitutions.

The methods, compositions, and trophic factor combinations of the present invention can also employ synthetic non-peptide compositions that have biological activity functionally comparable to that of known defensin peptides. By functionally comparable, it is meant that the shape, size, flexibility, and electronic configuration of the non-peptide molecule is such that the biological activity of the molecule is similar to defensin peptides. In particular, the non-peptide molecules should display comparable mitogenic activity and/or antimicrobial activity or pore forming ability, preferably possessing both activities. Such non-peptide molecules will typically be small molecules having a molecular weight in the range from about 100 to about 1000 daltons. The use of such small molecules is frequently advantageous in the preparation of trophic factor combinations. Candidate mimetics can be screened in large numbers to identify those having the desired activity.

The identification of such nonpeptide analog molecules can be performed using techniques known in the art of drug design. Such techniques include, but are not limited to, self-consistent field (SCF) analysis, configuration interaction (CI) analysis, and normal mode dynamics computer analysis, all of which are well described in the scientific literature (e.g., Rein et al., Computer-Assisted Modeling of Receptor-Ligand Interactions, Alan Liss, N.Y., [1989]). Preparation of the identified compounds will depend on the desired characteristics of the compounds and will involve standard chemical synthetic techniques (e.g., Cary et al., Advanced Organic Chemistry, part B, Plenum Press, New York [1983]).

In some embodiments of the present invention, one or more substances having an effect that an antimicrobial peptide has can be used. Effects that antimicrobial peptides have include, but are not limited to, the following: form pores on the cell membrane; enter cells without membrane lysis and, once in the cytoplasm, bind to, and inhibit the activity of specific molecular targets essential to bacterial growth, thereby causing cell death; induce expression of syndecan, an integral membrane proteoglycan associated largely with epithelial cells, in mesenchymal cells and inhibit the NADPH oxidase activity of neutrophils, suggesting a role of this peptide in wound repair and inflammation; exert a protective effect in various animal models of ischemia-reperfusion injury, preventing the post-ischemic oxidant production; induce angiogenesis both in vitro and in vivo; inhibit membrane protein synthesis; inhibit DNA synthesis; antitumor effect; stimulate cell proliferation; interfere with signal pathways; chemoattractant for immune cells; stimulate cytokine expression; stimulate adhesion molecule expression; angiogenesis; and chloride secretion.

TABLE 1 Human Antimicrobial Peptides SEQ ID Organism NO: Protein Name Name Length Sequence 1 Antibacterial Homo 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYK peptide LL-37 sapiens EAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPD precursor TPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKR CMGTVNLNQARGSFDISCDKDNKRFALLGDFFRKS KEKIGKEFKRIVQRIKDFLRNLVPRTES 2 Antibacterial Homo 170 MKTQRDGHSLGRWSLVLLLLGLVMPLAIIAQVLSYK protein FALL-39 sapiens EAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPD precursor TPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKR CMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKS KEKIGKEFKRIVQRIKDFLRNLVPRTES 3 Antimicrobial Homo 476 MQPVMLALWSLLLLWGLATPCQELLETVGTLARIDK peptide RYA3 sapiens DELGKAIQNSLVGEPILQNVLGSVTAVNRGLLGSGG LLGGGGLLGHGGVFGVVEELSGLKIEELTLPKVLLKL LPGFGVQLSLHTKVGMHCSGPLGGLLQLAAEVNVT SRVALAVSSRGTPILILKRCSTLLGHISLFSGLLPTPL FGVVEQMLFKVLPGLLCPVVDSVLGVVNELLGAVLG LVSLGALGSVEFSLATLPLISNQYIELDINPIVKSVAG DIIDFPKSRAPAKVPPKKDHTSQVMVPLYLFNTTFGL LQTNGALDMDITPELVPSDVPLTTTDLAALLPEALGK LPLHQQLLLFLRVREAPTVTLHNKKALVSLPANIHVL FYVPKGTPESLFELNSVMTVRAQLAPSATKLHISLSL ERLSVKVASSFTHAFDGSRLEEWLSHVVGAVYAPK LNVALDVGIPLPKVLNINFSNSVLEIVENAVVLTVAS 4 Azurocidin Homo 251 MTRLTVLALLAGLLASSRAGSSPLLDIVGGRKARPR precursor sapiens QFPFLASIQNQGRHFCGGALIHARFVMTAASCFQS QNPGVSTVVLGAYDLRRRERQSRQTFSISSMSENG YDPQQNLNDLMLLQLDREANLTSSVTILPLPLQNAT VEAGTRCQVAGWGSQRSGGRLSRFPRFVNVTVTP EDQCRPNNVCTGVLTRRGGICNGDGGTPLVCEGLA HGVASFSLGPCGRGPDFFTRVALFRDWIDGVLNNP GPGPA 5 Bactericidal Homo 483 MARGPCNAPRWVSLMVLVAIGTAVTAAVNPGVVVR permeability- sapiens ISQKGLDYASQQGTAALQKELKRIKIPDYSDSFKIKH increasing LGKGHYSFYSMDIREFQLPSSQISMVPNVGLKFSIS protein NANIKISGKWKAQKRFLKMSGNFDLSIEGMSISADL precursor (BPI) KLGSNPTSGKPTITCSSCSSHINSVHVHISKSKVGW (CAP 57) LIQLFHKKIESALRNKMNSQVCEKVTNSVSSKLQPY FQTLPVMTKIDSVAGINYGLVAPPATTAETLDVQMK GEFYSENHHNPPPFAPPVMEFPAAHDRMVYLGLSD YFFNTAGLVYQEAGVLKMTLRDDMIPKESKFRLTTK FFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQPTGL TFYPAVDVQAFAVLPNSSLASLFLIGMHTTGSMEVS AESNRLVGELKLDRLLLELKHSNIGPFPVELLQDIMN YIVPILVLPRVNEKLQKGFPLPTPARVQLYNVVLQPH QNFLLFGADVVYK 6 bactericidal/permeability- Homo 487 MRENMARGPCNAPRWVSLMVLVAIGTAVTAAVNP increasing sapiens GVVVRISQKGLDYASQQGTAALQKELKRIKIPDYSD protein SFKIKHLGKGHYSFYSMDIREFQLPSSQISMVPNVG precursor LKFSISNANIKISGKWKAQKRFLKMSGNFDLSIEGMS ISADLKLGSNPTSGKPTITCSSCSSHINSVHVHISKS KVGWLIQLFHKKIESALRNKMNSQVCEKVTNSVSSK LQPYFQTLPVMTKIDSVAGINYGLVAPPATTAETLDV QMKGEFYSENHHNPPPFAPPVMEFPAAHDRMVYL GLSDYFFNTAGLVYQEAGVLKMTLRDDMIPKESKFR LTTKFFGTFLPEVAKKFPNMKIQIHVSASTPPHLSVQ PTGLTFYPAVDVQAFAVLPNSSLASLFLIGMHTTGS MEVSAESNRLVGELKLDRLLLELKHSNIGPFPVELL QDIMNYIVPILVLPRVNEKLQKGFPLPTPARVQLYNV VLQPHQNFLLFGADVVYK 7 beta defensin Homo 111 MKSLLFTLAVFMLLAQLVSGNWYVKKCLNDVGICKK 126 sapiens KCKPEEMHVKNGWAMCGKQRDCCVPADRRANYP preproprotein; VFCVQTKTTRISTVTATTATTTLMMTTASMSSMAPT epididymal PVSPTG secretory protein ESP13.2; beta defensin 26; chromosome 20 open reading frame 8 8 beta-defensin Homo 65 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGTCKNN sapiens CGKNEELIALCQKFLKCCRTIQPCGSIID 9 Beta-defensin Homo 67 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYCRVRG 103 precursor sapiens GRCAVLSCLPKEEQIGKCSTRGRKCCRRKK (Beta-defensin 3) (DEFB-3) (BD-3) (hBD-3) (HBD3) (Defensin like protein) 10 Beta-defensin Homo 72 MQRLVLLLAVSLLLYQDLPVRSEFELDRICGYGTAR 104 precursor sapiens CRKKCRSQEYRIGRCPNTYACCLRKWDESLLNRTKP (Beta-defensin 4) (DEFB-4) (BD-4) (hBD-4) 11 beta-defensin Homo 77 MALIRKTFYFLFAMFFILVQLPSGCQAGLDFSQPFPS 105 sapiens GEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFL CCRQR 12 Beta-defensin Homo 78 MALIRKTFYFLFAMFFILVQLPSGCQAGLDFSQPFPS 105 precursor sapiens GEFAVCESCKLGRGKCRKECLENEKPDGNCRLNFL (Beta-defensin CCRQRI 5) (DEFB-5) (BD-5) 13 beta-defensin Homo 57 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGTCKNN 106 sapiens CGKNEELIALCQKSLKCCRTI 14 Beta-defensin Homo 65 MRTFLFLFAVLFFLTPAKNAFFDEKCNKLKGTCKNN 106 precursor sapiens CGKNEELIALCQKSLKCCRTIQPCGSIID (Beta-defensin 6) (DEFB-6) (BD-6) 15 Beta-defensin Homo 63 MKIFVFILAALILLAQIFQARTAIHRALISKRMEGHCEA 107 precursor sapiens ECLTFEVKIGGCRAELAPFCCKNR (Beta-defensin 7) (DEFB-7) (Fragment) 16 beta-defensin Homo 59 MRIAVLFFTIFFFMSQVLPAKGKFKEICERPNGSCRD 108 sapiens FCLETEIHVGRCLNSRPCCLPL 17 Beta-defensin Homo 73 MRIAVLLFAIFFFMSQVLPARGKFKEICERPNGSCRD 108 precursor sapiens FCLETEIHVGRCLNSQPCCLPLGHQPRIESTTPKKD (Beta-defensin 8) (DEFB-8) 18 Beta-defensin Homo 123 MKLLLLALPMLVLLPQVIPAYSGEKKCWNRSGHCRK 118 precursor sapiens QCKDGEAVKDTCKNLRACCIPSNEDHRRVPATSPT (Beta-defensin PLSDSTPGIIDDILTVRFTTDYFEVSSKKDMVEESEA 18) (DEFB-18) GRGTETSLPNVHHSS (Epididymal secretory protein 13.6) (ESP13.6) 19 Beta-defensin Homo 84 MKLLYLFLAILLAIEEPXISGKRHILRCMGNSGICRAS 119 precursor sapiens CKKNEQPYLYCRNCQSCCLQSYMRISISGKEENTD (Beta-defensin WSYEKQWPRLP 19) (DEFB-19) 20 Beta-defensin Homo 88 MKLLYLFLAILLAIEEPVISVECWMDGHCRLLCKDGE 120 precursor sapiens DSIIRCRNRKRCCVPSRYLTIQPVTIHGILGWTTPQM (Beta-defensin STTAPKMKTNITNR 20) (DEFB-20) 21 Beta-defensin Homo 67 MKLLLLTLTVLLLLSQLTPGGTQRCWNLYGKCRYRC 123 precursor sapiens SKKERVYVYCINNKMCCVKPKYQPKERWVVPF (Beta-defensin 23) (DEFB-23) 22 Beta-defensin Homo 43 EFKRCWKGQGACQTYCTRQETYMHLCPDASLCCL 124 (Beta- sapiens SYALKPPPV defensin 24) (DEFB-24) (Fragment) 23 Beta-defensin Homo 152 MLTFIICGLLTRVTKGSFEPQKCWKNNVGHCRRRCL 125 precursor sapiens DTERYILLCRNKLSCCISIISHEYTRRPAFPVIHLEDIT (Beta-defensin LDYSDVDSFTGSPVSMLNDLITFDTTKFGETMTPET 25) (DEFB-25) NTPETTMPPSEATTPETTMPPSETATSETMPPPSQ TALTHN 24 Beta-defensin Homo 111 MKFLLFTLAVFMLLAQLVSGNWYVKKCLNDVGICKK 126 precursor sapiens KCKPEEMHVKNGWAMCGKQRDCCVPADRRANYP (Beta-defensin VFCVQTKTTRISTVTATTATTTLMMTTASMSSMAPT 26) (DEFB-26) PVSPTG (Epididymal secretory protein 13.2) (ESP13.2) 25 Beta-defensin Homo 99 MGLFMIIAILLFQKPTVTEQLKKCWNNYVQGHCRKIC 127 precursor sapiens RVNEVPEALCENGRYCCLNIKELEACKKITKPPRPK (Beta-defensin PATLALTLQDYVTIIENFPSLKTQST 27) (DEFB-27) 26 Beta-defensin Homo 183 MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLGRCRD 129 precursor sapiens HCNVDEKEIQKCKMKKCCVGPKVVKLIKNYLQYGTP (Beta-defensin NVLNEDVQEMLKPAKNSSAVIQRKHILSVLPQIKSTS 29) (DEFB-29) FFANTNFVIIPNATPMNSATISTMTPGQITYTATSTKS NTKESRDSATASPPPAPPPPNILPTPSLELEEAEEQ 27 Beta-defensin Homo 70 MRVLFFVFGVLSLMFTVPPGRSFISNDECPSEYYHC 131 precursor sapiens RLKCNADEHAIRYCADFSICCKLKIIEIDGQKKW (Beta-defensin 31) (DEFB-31) 28 Beta-Defensin 2 Homo 37 PVTCLKSGAICHPVFCPRRYKQIGTCGLPGTKCCKKP sapiens 29 Beta-defensin 2 Homo 64 MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKSGAI precursor (BD- sapiens CHPVFCPRRYKQIGTCGLPGTKCCKKP 2) (hBD-2) (Skin- antimicrobial peptide 1) (SAP1) 30 beta-defensin Homo 156 MNILMLTFIICGLLTRVTKGSFEPQKCWKNNVGHCR 25 precursor sapiens RRCLDTERYILLCRNKLSCCISIISHEYTRRPAFPVIH LEDITLDYSDVDSFTGSPVSMLNDLITFDTTKFGETM TPETNTPETTMPPSEATTPETTMPPSETATSETMPP PSQTALTHN 31 beta-defensin Homo 93 MKLFLVLIILLFEVLTDGARLKKCFNKVTGYCRKKCK 28 precursor sapiens VGERYEIGCLSGKLCCANDEEEKKHVSFKKPHQHS GEKLSVLQDYIILPTITIFTV 32 Beta-Defensin 3 Homo 45 GIINTLQKYYCRVRGGRCAVLSCLPKEEQIGKCSTR sapiens GRKCCRRKK 33 beta-defensin Homo 95 MKFLLLVLAALGFLTQVIPASAGGSKCVSNTPGYCR 32 precursor sapiens TCCHWGETALFMCNASRKCCISYSFLPKPDLPQLIG NHWQSRRRNTQRKDKKQQTTVTS 34 Beta-defensin-1 Homo 47 GNFLTGLGHRSDHYNCISSGGQCLYSACPIFTKIQG (Fragment) sapiens TCYRGKAKCCK 35 Beta-Defensin-2 Homo 41 GIGDPVTCLKSGAICHPVFCPRRYKQIGTCGLPGTK sapiens CCKKP 36 Beta-defensin-3 Homo 67 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYCRVRG sapiens GRCAVLSRLPKEEQIGKCSTRGRKCCRRKK 37 Calgranulin A Homo 93 MLTELEKALNSIIDVYHKYSLIKGNFHAVYRDDLKKLL (Migration sapiens ETECPQYIRKKGADVWFKELDINTDGAVNFQEFLILV inhibitory factor- IKMGVAAHKKSHEESHKE related protein 8) (MRP-8) (Cystic fibrosis antigen) (CFAG) (P8) (Leukocyte L1 complex light chain) (S100 calcium-binding protein A8) (Calprotectin L1L subun 38 Calgranulin B Homo 114 MTCKMSQLERNIETIINTFHQYSVKLGHPDTLNQGE (Migration sapiens FKELVRKDLQNFLKKENKNEKVIEHIMEDLDTNADK inhibitory factor- QLSFEEFIMLMARLTWASHEKMHEGDEGPGHHHK related protein PGLGEGTP 14) (MRP-14) (P14) (Leukocyte L1 complex heavy chain) (S100 calcium- binding protein A9) (Calprotectin L1H subunit) 39 Calgranulin C Homo 92 MTKLEEHLEGIVNIFHQYSVRKGHFDTLSKGELKQL (CAGC) sapiens LTKELANTIKNIKDKAVIDEIFQGLDANQDEQVDFQE (CGRP) FISLVAIALKAAHYHTHKE (Neutrophil S100 protein) (Calcium- binding protein in amniotic fluid 1) (CAAF1) (p6) [Contains: Calcitermin] 40 cathelicidin Homo 170 MKTQRNGHSLGRWSLVLLLLGLVMPLAIIAQVLSYK antimicrobial sapiens EAVLRAIDGINQRSSDANLYRLLDLDPRPTMDGDPD peptide TPKPVSFTVKETVCPRTTQQSPEDCDFKKDGLVKR CMGTVTLNQARGSFDISCDKDNKRFALLGDFFRKS KEKIGKEFKRIVQRIKDFLRNLVPRTES 41 Cathepsin G Homo 255 MQPLLLLLAFLLPTGAEAGEIIGGRESRPHSRPYMA precursor (EC sapiens YLQIQSPAGQSRCGGFLVREDFVLTAAHCWGSNIN 3.4.21.20) (CG) VTLGAHNIQRRENTQQHITARRAIRHPQYNQRTIQN DIMLLQLSRRVRRNRNVNPVALPRAQEGLRPGTLC TVAGWGRVSMRRGTDTLREVQLRVQRDRQCLRIF GSYDPRRQICVGDRRERKAAFKGDSGGPLLCNNVA HGIVSYGKSSGVPPEVFTRVSSFLPWIRTTMRSFKL LDQMETPL 42 chromogranin Homo 457 MRSAAVLALLLCAGQVTALPVNSPMNKGDTEVMKC A; parathyroid sapiens IVEVISDTLSKPSPMPVSQECFETLRGDERILSILRH secretory QNLLKELQDLALQGAKERAHQQKKHSGFEDELSEV protein 1 LENQSSQAELKEAVEEPSSKDVMEKREDSKEAEKS GEATDGARPQALPEPMQESKAEGNNQAPGEEEEE EEEATNTHPPASLPSQKYPGPQAEGDSEGLSQGLV DREKGLSAEPGWQAKREEEEEEEEEAEAGEEAVP EEEGPTVVLNPHPSLGYKEIRKGESRSEALAVDGA GKPGAEEAQDPEGKGEQEHSQQKEEEEEMAVVPQ GLFRGGKSGELEQEEERLSKEWEDSKRWSKMDQL AKELTAEKRLEGQEEEEDNRDSSMKLSFRARAYGF RGPGPQLRRGWRPSSREDSLEAGLPLQVRGYPEE KKEEEGSANRRPEDQELESLSAIEAELEKVAHQLQA LRRG 43 Defensin 5 Homo 94 MRTIAILAAILLVALQAQAESLQERADEATTQKQSGE precursor sapiens DNQDLAISFAGNGLSALRTSGSQARATCYCRTGRC (Defensin, ATRESLSGVCEISGRLYRLCCR alpha 5) 44 Defensin 6 Homo 101 MRTLTILTAVLLVALQAKAEPLQAEDDPLQAKAYEA sapiens DAQEQRGANDQDFAVSFAEDASSSLRALGGSTRAF TCHCRRSCYSTEYSYGTCTVMGINHRFCCL 45 Defensin 6 Homo 100 MRTLTILTAVLLVALQAKAEPLQAEDDPLQAKAYEA precursor sapiens DAQEQRGANDQDFAVSFAEDASSSLRALGSTRAFT (Defensin, CHCRRSCYSTEYSYGTCTVMGINHRFCCL alpha 6) 46 defensin alpha- Homo 65 CCSPGADCSGHPRSGCFPCMGRKLGSKASRLKEK 3 precursor sapiens HGLLLQNTSVHCRRTSLWNLHLPGKTLGILL (mistranslated) 47 defensin beta Homo 60 MKIFFFILAALILLAQIFQARTAIHRALISKRMEGHCEA 107 sapiens ECLTFEVKIGGCRAELAPFCC 48 defensin beta Homo 52 GKFKEICERPNGSCRDFCLETEIHVGRCLNSQPCCL 108 sapiens PLGHQPRIESTTPKKD 49 Defensin beta Homo 21 SCTAIGGRCKNQCDDSEFRIS 112 (Fragment) sapiens 50 Defensin beta Homo 39 KRYGRCKRDCLESEKQIDICSLPGKICCTEKLYEED 114 (Fragment) sapiens DMF 51 defensin beta Homo 101 GEKKCWNRSGXCRKQCKDGEAVKDTCKNXRACCI 118 sapiens PSNEDHRRVPATSPTPLSDSTPGIIDDILTVRFTTDY FEVSSKKDMVEESEAGRGTETSLPNVHHSS 52 defensin beta Homo 94 SLLFTLAVFMLLAQLVSGNWYVKKCLNDVGICKKC 126 sapiens KPEEMHVKNGWAMCGKQRDCCVPADRRANYPVF CVQTKTTRISTVTATTATTTLMMTT 53 defensin beta Homo 59 EQLKKCWNNYVQRHCRKICRVNEVPEALCENGRY 127 sapiens CCLNIKELEACKKITKPPSPKQHLH 54 defensin beta Homo 155 MKLLFPIFASLMLQYQVNTEFIGLRRCLMGLGRCRD 129 sapiens HCNVDEKEIQKCKMKKCCVGPKVVKLIKNYLQYGTP NVLNEDVQEMLKPAKNSSAVIQRKHILSVLPQIKSTS FFANTNFVIIPNATPMNSATISTMTPGQITYTATSTKS NTKESRDS 55 defensin beta-1 Homo 36 DHYNCVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK sapiens 56 Defensin HNP- Homo 30 DCYCRIPACIAGERRYGTCIYQGRLWAFCC 3 - Chain B sapiens 57 EP2E Homo 80 MKVFFLFAVLFCLVQTNSGDVPPGIRNTICRMQQGI sapiens CRLFFCHSGEKKRDICSDPWNRCCVSNTDEEGKEK PEMDGRSGI 58 gene TAP1 Homo 33 GYDTEVGEAGSQLSGGQRQAVALARALIRKPCV protein sapiens 59 Hepcidin Homo 84 MALSSQIWAACLLLLLLLASLTSGSVFPQQTGQLAE precursor sapiens LQPQDRAGARASWMPMFQRRRRRDTHFPICIFCC (Liver- GCCHRSKCGMCCKT expressed antimicrobial peptide) (LEAP- 1) (Putative liver tumor regressor) (PLTR) [Contains: Hepcidin 25 (Hepc25); Hepcidin 20 (Hepc20)] 60 High mobility Homo 215 MGKGDPKKPRGKMSSYAFFVQTCREEHKKKHPDA group protein 1 sapiens SVNFSEFSKKCSERWKTMSAKEKGKFEDMAKADK (HMG-1) ARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFL FCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAAD DKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKG VVKAEKSKKKKEEEEDEEDEEDEEEEEDEEDEDEE EDDDDE 61 liver-expressed Homo 81 MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAKRRPRR antimicrobial sapiens MTPFWRGVSLRPIGASCRDDSECITRLCRKGQQSP peptide 2 PTMLRSMEY isoform 62 Liver-expressed Homo 77 MWHLKLCAVLMIFLLLLGQIDGSPIPEVSSAKRRPRR antimicrobial sapiens MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSL peptide 2 SVAQE precursor (LEAP-2) 63 Lysozyme C Homo 148 MKALIVLGLVLLSVTVQGKVFERCELARTLKRLGMD precursor (EC sapiens GYRGISLANWMCLAKWESGYNTRATNYNAGDRST 3.2.1.17) (1,4- DYGIFQINSRYWCNDGKTPGAVNACHLSCSALLQD beta-N- NIADAVACAKRVVRDPQGIRAWVAWRNRCQNRDV acetylmuramidase RQYVQGCGV C) 64 Neutrophil Homo 94 MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIA defensin 1 sapiens ADIPEVVVSLAWDESLAPKHPGSRKNMACYCRIPA precursor CIAGERRYGTCIYQGRLWAFCC (HNP-1) (HP-1) (HP1) (Defensin, alpha 1) [Contains: HP 1-56; Neutrophil defensin 2 (HNP-2) (HP-2) (HP2)] 65 Neutrophil Homo 94 MRTLAILAAILLVALQAQAEPLQARADEVAAAPEQIA defensin 3 sapiens ADIPEVVVSLAWDESLAPKHPGSRKNMDCYCRIPA precursor CIAGERRYGTCIYQGRLWAFCC (HNP-3) (HP-3) (HP3) (Defensin, alpha 3) [Contains: HP 3-56; Neutrophil defensin 2 (HNP-2) (HP-2) (HP2)] 66 Neutrophil Homo 97 MRIIALLAAILLVALQVRAGPLQARGDEAPGQEQRG defensin 4 sapiens PEDQDISISFAWDKSSALQVSGSTRGMVCSCRLVF precursor CRRTELRVGNCLIGGVSFTYCCTRVD (HNP-4) (HP-4) (Defensin, alpha 4) 67 Retrocyclin Homo 56 MPCFSWWPCRLRRSHFRQELMKLQPRSSLEQMIR sapiens KWLMPLHGMKVPLFRFQTQREA 68 Ribonuclease 7 Homo 156 MAPARAGFCPLLLLLLLGLWVAEIPVSAKPKGMTSS precursor (EC sapiens QWFKIQHMQPSPQACNSAMKNINKHTKRCKDLNTF 3.1.27.—) LHEPFSSVAATCQTPKIACKNGDKNCHQSHGPVSL (RNase 7) TMCKLTSGKYPNCRYKEKRQNKSYVVACKPPQKK (Skin-derived DSQQFHLVPVHLDRVL antimicrobial protein 2) (SAP- 2) 69 Salivary gland Homo 46 MHDFWVLWVLLEYIYNSACSVLSATSSVSSRVLNR antimicrobial sapiens SLQVKVVKITN salvic 70 Secretogranin I Homo 677 MQPTLLLSLLGAVGLAAVNSMPVDNRNHNEGMVTR precursor (SgI) sapiens CIIEVLSNALSKSSAPPITPECRQVLKTSRKDVKDKE (Chromogranin TTENENTKFEVRLLRDPADASEAHESSSRGEAGAP B) (CgB) GEEDIQGPTKADTEKWAEGGGHSRERADEPQWSL [Contains: YPSDSQVSEEVKTRHSEKSQREDEEEEEGENYQK GAWK peptide; GERGEDSSEEKHLEEPGETQNAFLNERKQASAIKK CCB peptide] EELVARSETHAAGHSQEKTHSREKSSQESGEEAGS QENHPQESKGQPRSQEESEEGEEDATSEVDKRRT RPRHHHGRSRPDRSSQGGSLPSEEKGHPQEESEE SNVSMASLGEKRDHHSTHYRASEEEPEYGEEIKGY PGVQAPEDLEWERYRGRGSEEYRAPRPQSEESW DEEDKRNYPSLELDKMAHGYGEESEEERGLEPGK GRHHRGRGGEPRAYFMSDTREEKRFLGEGHHRVQ ENQMDKARRHPQGAWKELDRNYLNYGEEGAPGK WQQQGDLQDTKENREEARFQDKQYSSHHTAEKRK RLGELFNPYYDPLQWKSSHFERRDNMNDNFLEGE EENELTLNEKNFFPEYNYDWWEKKPFSEDVNWGY EKRNLARVPKLDLKRQYDRVAQLDQLLHYRKKSAE FPDFYDSEEPVSTHQEAENEKDRADQTVLTEDEKK ELENLAAMDLELQKIAEKFSQRG 71 Similar to Homo 226 AEGKWGLAHGRAEAHVWPGQGGWRLGPPQGRW azurocidin 1 sapiens TGSSPLLDIVGGRKARPRQFPFLASIQNQGRHFCG (Cationic GALIHARFVMTAASCFQSQNPGVSTVVLGAYDLRR antimicrobial RERQSRQTFSISSMSENGYDPQQNLNDLMLLQLDR protein 37) EANLTSSVTILPLPLQNATVEAGTRCQVAGWGSQR (Fragment) SGGRLSRFPRFVNVTVTPEDQCRPNNVCTGVLTRR GGICNVSAPCGGRRGPERY 72 11.5 kDa Carcinus 84 NKDCKYWCKDNLGLNYCCGQPGVTYPPFTKKHLG antibacterial maenas RCPAVRDTCTGVRTQLPTYCPHDGACQFRSKCCY protein DTCLKHHVCKTAEYPY 73 27 kDa Cyprinus 19 GIGGKPVQTAFVDNDGIYD antibacterial carpio protein (Fragment) 74 4 kDa defensin Androctonus 37 GFGCPFNQGACHRHCRSIRRRGGYCAGLFKQTCT australis CYR 75 4 kDa defensin Leiurus 38 GFGCPLNQGACHRHCRSIRRRGGYCAGFFKQTCT (Antibacterial 4 kDa quinquestriatus CYRN peptide) 76 7.5 kDa Ovis aries 164 METQMASPSLGRCSLWLLLLGLLLPSASAQALSYR bactinecin EAVLRAVGQLNEKSSEVNLYRLLELDPPPKDAEDQ (Fragment) GARKPVSFRVKETVCPRTSQQPPEQCDFKENGLVK QCVGTVSLDTSNDEFDLNCNELQSVRRLRPRRPRL PRPRPRPRPRPRSLPLPRPQPRRI 77 Abaecin Bombus 39 FVPYNPPRPGQSKPFPSFPGHGPFNPKIQWPYPLP pascuorum NPGH 78 Abaecin Apis 53 MKVVIFIFALLATICAAFAYVPLPNVPQPGRRPFPTF precursor mellifera PGQGPFNPKIKWPQGY 79 Acaloleptin A1 Acalolepta 71 SLQPGAPNVNNKDQPWQVSPHISRDDSGNTRTDIN luxuriosa VQRHGENNDFEAGWSKVVRGPNKAKPTWHIGGTH RW 80 Achacin Achatina 531 MLLLNSALFILCLVCWLPGTSSSRVLTRREGPQCSR precursor fulica SVDVAVVGAGPSGTYSAYKLRNKGQTVELFEYSNR IGGRLFTTHLPNVPDLNLESGGMRYFKNHHKIFGVL VKELNLSNKEFTEGFGKPGRTRFFARGKSLTLEEMT SGDVPYNLSTEEKANQANLAGYYLKKLTGFDGEVL TIPQANKLEVDDGRKLYQLTVDEALDKVGTPEGKEF LKAFSTGNTEFIEGVSAVNYFLVELGEREEEILTLTD GMSALPQALADAFLKSSTSHALTLNRKLQSLSKTDN GLYLLEFLETNTHEGYTEESNITDLVCARKVILAIPQS ALIHLDWKPLRSETVNEAFNAVKFIPTSKVFLTFPTA WWLSDAVKNPAFVVKSTSPFNQMYDWKSSNVTGD AAMIASYADTSDTKFQENLNSKGELIPGSAPGANRV TVALKEELLSQLSQAYGIERSDIPEPKSGTSQFWSS YPFEGDWTVWKAGYHCEYTQYIIERPSLIDDVFVVG SDHVNCIENAWTESAFLSVENVFEKYF 81 Acyl-CoA- Sus scrofa 87 MSQAEFEKAAEEVKNLKTKPADDEMLFIYSHYKQAT binding protein VGDINTERPGILDLKGKAKWDAWNGLKGTSKEDAM (ACBP) KAYINKVEELKKKYGI (Diazepam binding inhibitor) (DBI) (Endozepine) (EP) [Contains: DBI(32-86)] 82 Adenoregulin Phyllomedusa 81 MAFLKKSLFLVLFLGLVSLSICEEEKRENEDEEEQED precursor bicolor DEQSEMKRGLWSKIKEVGKEAAKAAAKAAGKAALG (Dermaseptin AVSEAVGEQ BII) (Dermaseptin B2) 83 Alpha-defensin 1 Macaca 96 MRTLAILAAILLVALQAQAEPLQARTDEATAAQEQIP mulatta TDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRI PACLAGERRYGTCFYMGRVWAFCC 84 Alpha-defensin Macaca 96 MRTLAILAAILLVALQAQAEPLQARTDEATAAQEQIP 1A mulatta TDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRI PACLAGERRYGTCFYLGRVWAFCC 85 Alpha-defensin 2 Macaca 94 MRTLAILAAILLFALLAQAKSLQETADDAATQEQPGE mulatta DDQDLAVSFEENGLSTLRASGSQARRTCRCRFGR CFRRESYSGSCNINGRIFSLCCR 86 Alpha-S2 Bos taurus 222 MKFFIFTCLLAVALAKNTMEHVSSSEESIISQETYKQ casein EKNMAINPSKENLCSTFCKEVVRNANEEEYSIGSSS precursor EESAEVATEEVKITVDDKHYQKALNEINQFYQKFPQ [Contains: YLQYLYQGPIVLNPWDQVKRNAVPITPTLNREQLST Casocidin-I] SEENSKKTVDMESTEVFTKKTKLTEEEKNRLNFLKKI SQRYQKFALPQYLKTVYQHQKAMKPWIQPKTKVIP YVRYL 87 Androctonin Androctonus 25 RSVCRQIKICRRRGGCYYKCTNRPY australis 88 Andropin Drosophila 57 MKYFVVLVVLALILAITVGPSDAVFIDILDKMENAIHK precursor mauritiana AAQAGIGIAKPIEKMILPK 89 Andropin Drosophila 57 MKYFVVLVVLALILAISVGPSDAVFIDILDKVENAIHNA precursor melanogaster AQVGIGFAKPFEKLINPK 90 Andropin Drosophila 67 MKYFLVLVVLTLILAISVGQSDALFVDIIDNVENAIHKA precursor orena AKTGIGMVKPIENIFIPNQQKKSTEASN 91 Andropin Drosophila 57 MKYFVVLVVLALILAITVDPSDAVFIDILDKMENAIHKA precursor sechellia AQAGIGLAKPIENMILPK 92 Andropin Drosophila 60 MKYFVVLVVLALILAIAVGPSDAVFIDILDKMENAIHK precursor simulans AAQAGIGIAKPIENMILPKLTK 93 Andropin Drosophila 62 MKYFSVLVVLTLILAIVDQSDAFINLLDKVEDALHTGA precursor teissieri QAGFKLIRPVERGATPKKSEKPEK 94 Andropin Drosophila 60 MKYFSVLVVLTLILAISVGQSNAIFVDVLDNVETALHN precursor yakuba AAKAGFKLIKPIEKMIMPSKEK 95 Anionic Bombina 144 MNFKYIFAVSFLIASAYARSVQNDEQSLSQRDVLEE antimicrobial maxima ESLREIRGIGGKILSGLKTALKGAAKELASTYLHRKR peptide TAEEHEEMKRLEAVMRDLDSLDYPEEASERETRGF NQDEIANLFTKKEKRILGPVLGLVSDTLDDVLGILG 96 Antibacterial 6.5 kDa Carcinus 30 XXVPYPRPFPRPPIGPRPLPFPGGGRPFQS protein maenas (Fragment) 97 Antibacterial Bos taurus 158 METQRASLSLGRWSLWLLLLGLALPSASAQALSYR peptide BMAP- EAVLRAVDQFNERSSEANLYRLLELDPPPKEDDEN 27 precursor PNIPKPVSFRVKETVCPRTSQQPAEQCDFKENGLV (Myeloid KQCVGTVTLDAVKGKINVTCEELQSVGRFKRFRKKF antibacterial KKLFKKLSPVIPLLHLG peptide 27) 98 Antibacterial Bos taurus 159 METQRASLSLGRWSLWLLLLGLALPSASAQALSYR peptide BMAP- EAVLRAVDQLNEKSSEANLYRLLELDPPPKEDDENP 28 precursor NIPKPVSFRVKETVCPRTSQQSPEQCDFKENGLLKE (Myeloid CVGTVTLDQVGSNFDITCAVPQSVGGLRSLGRKILR antibacterial AWKKYGPIIVPIIRIG peptide 28) 99 Antibacterial Bos taurus 165 METQRASFSLGRSSLWLLLLGLVVPSASAQDLSYR peptide BMAP- EAVLRAVDQFNERSSEANLYRLLELDPPPEQDVEH 34 precursor PGARKPVSFTVKETVCPRTTPQPPEQCDFKENGLV KQCVGTVTRYWIRGDFDITCNNIQSAGLFRRLRDSI RRGQQKILEKARRIGERIKDIFRG 100 Antibacterial Bombyx 59 MNFTRIIFFLFVVVFATASGKPWNIFKEIERAVARTR peptide enbocin mori DAVISAGPAVRTVAAATSVASG precursor (Moricin) 101 Antibacterial Sus scrofa 153 METQRASLCLGRWSLWLLLLGLVVPSASAQALSYR peptide PMAP- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 23 precursor GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK (Myeloid QCVGTVTLKEIRGNFDITCNQLQSVRIIDLLWRVRRP antibacterial QKPKFVTVWVR peptide 23) 102 Antibacterial Sus scrofa 166 METQRASLCLGRWSLWLLLLGLVVPSASAQALSYR peptide PMAP- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 36 precursor GTPKPVSFTVKETVCPRPTWRPPELCDFKENGRVK (Myeloid QCVGTVTLNPSNDPLDINCDEIQSVGRFRRLRKKTR antibacterial KRLKKIGKVLKWIPPIVGSIPLGCG peptide 36) 103 Antibacterial Sus scrofa 167 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR peptide PMAP- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 37 precursor GTPKPVSFTVKETVCPRPTWRPPELCDFKENGRVK (Myeloid QCVGTVTLDQIKDPLDITCNEIQSVGLLSRLRDFLSD antibacterial RGRRLGEKIERIGQKIKDLSEFFQS peptide 37) 104 Antibacterial Carcinus 88 GLFPNKDCKYWCKDNLGLNYCCGQPGVTYPPFTK protein 11.5 kDa maenas KHLGRCPAVRDTCTGVRTQLPTYCPHDGACQFRS (Fragment) KCCYDTCLKHHVCKTAEYPY 105 Antibacterial Sus scrofa 172 METQRASLCLGRWSLWLLLLGLVVPSASAQALSYR protein PR-39 EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP precursor GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLNPSIHSLDISCNEIQSVRRRPRPPYLPRP RPPPFFPPRLPPRIPPGFPPRFPPRFPGKR 106 antibacterial Sus scrofa 172 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR protein EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP precursor GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLNPSIHSLDISCNEIQSVRRRPRPPYLPRP RPPPFFPPRLPPRIPPGFPPRFPPRFPGKR 107 antibacterial Cavia 42 GLRKKFRKTRKRIQKLGRKIGKTGRKVXKAWREYG protein, 11K porcellus QIPYPCR 108 Antifungal Galleria 76 MKIAFIVAISLAFLAVTSCIEFEKSTESHDIQKRGVTIT peptide mellonella VKPPFPGCVFYECIANCRSRGYKNGGYCTINGCQC gallerimycin LR 109 Antifungal Sarcophaga 85 MVKLFVIVILALIAVAFGQHGHGGQDQHGYGHGQQ protein peregrina AVYGKGHEGHGVNNLGQDGHGQHGYAHGHSDQH precursor (AFP) GHGGQHGQHDGYKNRGY 110 Antimicrobial Xenopus 66 LKCVNLQANGIKMTQECAKEDTKCLTLRSLKKTLKF amphipathic laevis CASGRTCTTMKIMSLPGEQITCCEGNMCNA helix-forming peptide 111 Antimicrobial Acrocinus 34 CIKNGNGCQPDGSQGNCCSRYCHKEPGWVAGYCR peptide ALO1 longimanus 112 Antimicrobial Acrocinus 34 CIANRNGCQPDGSQGNCCSGYCHKEPGWVAGYC peptide ALO2 longimanus 113 Antimicrobial Acrocinus 36 CIKNGNGCQPNGSQGNCCSGYCHKQPGWVAGYC peptide ALO3 longimanus RRK 114 Antimicrobial Glossina 208 MQSFKICFFISCLSVVLVKGQFGGTVSSNPNGGLDV peptide attacin morsitans NARLSKTIGDPNANVVGGVFAAGNTDGGPATRGAF AttA LAANKDGHGLSLQHSKTDNFGSSLTSSAHAHLFND KTHKLDANAFHSRTHLDNGFKFDRVGGGLRYDHVT GHGASLTASRIPQLDMNTLGLTGKANLWSSPNRAT TLDLTGGVSKHFGGPFDGQTNKQIGLGLNSRF 115 Antimicrobial Manduca 67 MKFSRVLFFVFACFAAFTVTAAKPWDFLKELEGAG peptide sexta QRIRDAIISAQPAVETIAQATAIFKGQSKEED cecropin 6 116 Antimicrobial Gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCK peptide CHP1 gallus RIR (Chicken heterophil peptide 1) 117 Antimicrobial Gallus 34 GRKSDCFRKNGFCAFLKCPYLTLISGLCSXFHLC peptide CHP2 gallus (Chicken heterophil peptide 2) (Fragment) 118 Antimicrobial Glossina 87 MKFYLVLAFLTLCAVAVTALPAGDETRIDLETLEEDL peptide morsitans RLVDGAQVTGELKRDKRVTCNIGEWVCVAHCNSKS defensin DefA KKSGYCSRGVCYCTN 119 Antimicrobial Glossina 76 PQSPPAQIKDPKIYASGGGSPKDGYNVNVDVRKNV peptide morsitans WVSQNGRHSIDATGGYSQHLGGPYGNSRPDFRGG diptericin DipA ASYTYRE (Fragment) 120 Antimicrobial Equus 46 DVQCGEGHFCHDXQTCCRASQGGXACCPYSQGV peptide eNAP-1 caballus CCADQRHCCPVGF (Fragment) 121 Antimicrobial Equus 46 EVERKHPLGGSRPGRCPTVPPGTFGHCACLCTGD peptide eNAP-2 caballus ASEPKGQKCCSN (Fragment) 122 Antimicrobial Manduca 171 AILFAAIVACACAQVSMPPQYAQIYPEYYKYSKQVR peptide gloverin sexta HPRDVTWDKQVGNNGKVFGTLGQNDQGLFGKGG (Fragment) YQHQFFDDHRGKLTGQGYGSRVLGPYGDSTNFGG RLDWANKNANAALDVTKSIGGRTGLTASGSGVWQL GKNTDLSAGGTLSQTLGHGKPDVGFQGLFQHRW 123 Antimicrobial Sus scrofa 82 MALSVQIRAACLLLLLLVSLTAGSVLPSQTRQLTDLR peptide TQDTAGATAGLTPVAQRLRRDTHFPICIFCCGCCRK hepcidin AICGMCCKT 124 Antimicrobial Lumbricus 76 MSLCISDYLYLTLTFSKYERQKDKRPYSERKNQYTG peptide rubellus PQFLYPPERIPPQKVIKWNEEGLPIYEIPGEGGHAEP lumbricin1 AAA 125 Antimicrobial Mytilus 82 MKAVFVLLVVGLCIMMMDVATAGFGCPNNYACHQH peptide MGD2b galloprovincialis CKSIRGYCGGYCASWFRLRCTCYRCGGRRDDVEDI FDIYDNVAVERF 126 Antimicrobial Manduca 67 MKLTSLFIFVIVALSLLFSSTDAAPGKIPVKAIKQAGK peptide moricin sexta VIGKGLRAINIAGTTHDVVSFFRPKKKKH 127 Antimicrobial Equus 160 MKKMGCGGRLSSCPTMTSRALLLLASALLGTPGLT peptide NK- caballus FSGLNPESYDLATAHLSDGEQFCQGLTQEDLQGDL lysin LTERERQGIACWSCRKILQKLEDLVGEQPNEATINE AASRVCRNLGLLRGACKKIMRTCLRLISRDILAGKKP QEVCVDIKLCKHKAGLI 128 Antimicrobial Xenopus 24 GVLSNVIGYLKKLGTGALNAVLKQ peptide PGQ laevis 129 Antimicrobial Meleagris 65 MRIVYLLFPFILLLAQGAAGSSLALGKREKCLRRNGF peptide THP1 gallopavo CAFLKCPTLSVISGTCSRFQVCCKTLLG precursor (Turkey heterophil peptide 1) 130 Antimicrobial Meleagris 64 MRILYLLFSLLFLALQVSPGLSSPKRDMLFCKRGTC peptide THP2 gallopavo HFGRCPSHLIKVGSCFGFRSCCKWPWDA precursor (Turkey heterophil peptide 2) 131 Antimicrobial Meleagris 25 LSCKRGTCHFGRCPSHLIKGSCSGG peptide THP3 gallopavo (Turkey heterophil peptide 3) (Fragment) 132 Antimicrobial Manduca 207 KMFTKFVVLVCLLVGAKARPQLGALTFNSDGTSGA protein attacin 2 sexta AVKVPFGGNKNNIFSAIGGADFNANHKLSSATAGVA (Fragment) LDNIRGHGLSLTDTHIPGFGDKLTAAGKLNLFHNNN HDLTANAFATRNMPNIPQVPNFNTVGGGLDYMFKN KVGASLGAAHTDFINRNDYSVGGKLNLFRNPSTSLD FNAGFKKFDTPFMRSGWEPNMGFSLSKFF 133 Antimicrobial Oryctolagus 171 METHKHGPSLAWWSLLLLLLGLLMPPAIAQDLTYRE protein CAP18 cuniculus AVLRAVDAFNQQSSEANLYRLLSMDPQQLEDAKPY precursor (18 kDa TPQPVSFTVKETECPRTTWKLPEQCDFKEDGLVKR lipopolysaccharide- CVGTVTRYQAWDSFDIRCNRAQESPEPTGLRKRLR binding KFRNKIKEKLKKIGQKIQGFVPKLAPRTDY protein) (18 kDa cationic protein) CAP18-A 134 Antimicrobial- Pheretima 67 MYSKYERQKDKRPYSERKDQYTGPQFLYPPDRIPP like peptide PP-1 tschiliensis SKAIKWNEEGLPMYEVLPDGAGAKTAVEAAAE 135 Apidaecin Bombus 17 GNRPVYIPPPRPPHPRL pascuorum 136 apidaecin lb Apis 26 EAKPEAKPGNNRPVYIPQPRPPHPRL precursor mellifera 137 Apidaecin Apis 168 MKNFALAILVVTFVVAVFGNTNLDPPTRPARLRREA precursor, type mellifera KPEAEPGNNRPIYIPQPRPPHPRLRREAEPKAEPGN 14 NRPIYIPQPRPPHPRLRREAESEAEPGNNRPVYIPQ PRPPHPRLRREPEAEPGNNRPVYIPQPRPPHPRLR REPEAEPGNNRPVYIPQPRPPHPRI 138 Apidaecin Apis 144 MKNFALAILVVTFVVAVFGNTNLDPPTRPTRLRREA precursor, type mellifera EPEAEPGNNRPVYIPQPRPPHPRLRREAEPEAEPG 22 NNRPVYIPQPRPPHPRLRREAEPEAEPGNNRPVYIP QPRPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHP RI 139 Apidaecin Apis 283 KNFALAILVVTFVVAVFGNTNLDPPTRPTRLRREAKP precursor, type mellifera EAEPGNNRPVYIPQPRPPHPRLRREAEPEAEPGNN 73 (Fragment) RPVYIPQPRPPHPRLRREAELEAEPGNNRPVYISQP RPPHPRLRREAEPEAEPGNNRPVYIPQPRPPHPRL RREAELEAEPGNNRPVYISQPRPPHPRLRREAEPE AEPGNNRPVYIPQPRPPHPRLRREAEPEAEPGNNR PVYIPQPRPPHPRLRREAEPEAEPGNNRPVYIPQPR PPHPRLRREAKPEAKPGNNRPVYIPQPRPPHPRI 140 Apolipoprotein Bos taurus 76 QAEESNLQSLVSQYFQTVADYGKDLVEKAKGSELQ A-II (Apo-AII) TQAKAYFEKTQEELTPFFKKAGTDLLNFLSSFIDPKK (Antimicrobial QPAT peptide BAMP- 1) 141 ASABF Ascaris 93 MKTAIIVVLLVIFASTNAAVDFSSCARMDVPGLSKVA precursor suum QGLCISSCKFQNCGTGHCEKRGGRPTCVCDRCGR (ASABF-alpha) GGGEWPSVPMPKGRSSRGRRHS 142 ASABF-epsilon Ascaris 65 MVTKGIVLFMLVILFASTDAATCGYDDAKLNRPTIGC (ASABF suum ILSCKVQGCETGACYLRDSRPICVCKRC epsilon2) 143 ASABF-zeta Ascaris 94 MKAILIALLLTTFTVVNGGVVLTSCARMDTPVLSKAA suum QGLCITSCKYQNCGTGFCQKVGGRPTCMCRRCAN GGGSWPVIPLDTLVKLALKRGKR 144 ASABF-zeta2 Ascaris 35 TSCKYQNCGTGFCQKVGGRPTCMCRRCANGGGS (Fragment) suum WP 145 Attacin A Drosophila 224 MQKTSILIVALVALFAITEALPSLPTTGPIRVRRQVLG precursor melanogaster GSLTSNPAGGADARLDLTKGIGNPNHNVVGQVFAA GNTQSGPVTTGGTLAYNNAGHGASLTKTHTPGVKD VFQQEAHANLFNNGRHNLDAKVFASQNKLANGFEF QRNGAGLDYSHINGHGASLTHSNFPGIGQQLGLDG RANLWSSPNRATTLDLTGSASKWTSGPFANQKPNF GAGLGLSHHFG 146 Attacin A Trichoplusia 254 MFTYKLILGLVLVVSASARYLVFEDLEGESYLVPNQA precursor ni EDEQVLEGEPFYENAVQLASPRVRRQAQGSVTLNS DGSMGLGAKVPIVGNEKNVLSALGSVDLNDQLKPA SRGMGLALDNVNGHGLSVMKETVPGFGDRLTGAG RVNVFHNDNHDISAKAFVTKNMPDFPNVPNFNTVG GGVDYMYKNKVGASLGMANTPFLDRKDYSAMGNL NVFRSPTTSVDFNAGFKKFDTPVFKSNWEPNFGLT FSRSFGNKW 147 Attacin B Drosophila 218 MQKTSILILALFAIAEAVPTTGPIRVRRQVLGGSLASN precursor melanogaster PAGGADARLNLSKGIGNPNHNVVGQVFAAGNTQS GPVTTGGTLAYNNAGHGASLTKTHTPGVKDVFQQE AHANLFNNGRHNLDAKVFASQNKLANGFEFQRNGA GLDYSHINGHGASLTHSNFPGIGQQLGLDGRANLW SSPNRATTLDLTGSASKWTSGPFANQKPNFGAGLG LSHHFG 148 Attacin B Hyalophora 233 MFAKLFLVSVLLVGVNSRYVLVEEPGYYDKQYEEQ precursor cecropia PQQWVNSRVRRQAGALTINSDGTSGAVVKVPITGN (Immune ENHKFSALGSVDLTNQMKLGAATAGLAYDNVNGHG protein P5) ATLTKTHIPGFGDKMTAAGKVNLFHNDNHDFSAKAF ATKNMPNIPQVPNFNTVGAGVDYMFKDKIGASANA AHTDFINRNDYSLGGKLNLFKTPTTSLDFNAGWKKF DTPFFKSSWEPSTSFSFSKYF 149 Attacin E and F Hyalophora 235 MFGKIVFLLLVALCAGVQSRYLIVSEPVYYIEHYEEP precursor cecropia ELLASSRVRRDAHGALTLNSDGTSGAVVKVPFAGN (Immune DKNIVSAIGSVDLTDRQKLGAATAGVALDNINGHGL protein P5) SLTDTHIPGFGDKMTAAGKVNVFHNDNHDITAKAFA TRNMPDIANVPNFNTVGGGIDYMFKDKIGASASAAH TDFINRNDYSLDGKLNLFKTPDTSIDFNAGFKKFDTP FMKSSWEPNFGFSLSKYF 150 Attacin Bombyx 214 MSKSVALLLLCACLASGRHVPTRARRQAGSFTVNS precursor mori DGTSGAALKVPLTGNDKNVLSAIGSADFNDRHKLSA (Nuecin) ASAGLALDNVNGHGLSLTGTRIPGFGEQLGVAGKV NLFHNNNHDLSAKAFAIRNSPSAIPNAPNFNTLGGG VDYMFKQKVGASLSAAHSDVINRNDYSAGGKLNLF RSPSSSLDFNAGFKKFDTPFYRSSWEPNVGFSFSK FF 151 Attacin-A Drosophila 221 MQNTSILIVALVALFAITEALPTTGPIRVRRQVLGGSL CG10146-PA melanogaster TSNPAGGADARLDLTKGIGNPNHNVVGQVFAAGNT QSGPVTTGGTLAYNNAGHGASLTKTHTPGVKDVFQ QEAHANLFNNGRHNLDAKVFASQNKLANGFEFQRN GAGLDYSHINGHGASLTHSNFPGIGQQLGLDGRAN LWSSPNRATTLDLTGSASKWTSGPFANQKPNFGA GLGLSHHFG 152 Attacin-B Drosophila 218 MQKTSILILALFAIAEAVPTTGPIRVRRQVLGGSLASN CG18372-PA melanogaster PAGGADARLNLSKGIGNPNHNVVGQVFAAGNTQS GPVTTGGTLAYNNAGHGASLTKTHTPGVKDVFQQE AHANLFNNGRHNLDAKVFASQNKLANGFEFQRNGA GLDYSHINGHGGSLTHSNFPGIGQQLGLDGRANLW SSPNRATTLDLTGSASKWTSGPFANQKPNFGAGLG LSHHFG 153 Azurocidin Sus scrofa 219 IVGGRRAQPQEFPFLASIQKQGRPFCAGALVHPRFV (Cationic LTAASCFRGKNSGSASVVLGAYDLRQQEQSRQTFS antimicrobial IRSISQNGYDPRQNLNDVLLLQLDREARLTPSVALV protein CAP37) PLPPQNATVEAGTNCQVAGWGTQRLRRLFSRFPR (Heparin- VLNVTVTSNPCLPRDMCIGVFSRRGRISQGDRGTPL binding protein) VCNGLAQGVASFLRRRFRRSSGFFTRVALFRNWID (HBP) SVLNNPP 154 bactenecin 5 Bos taurus 42 RFRPPIRRPPIRPPFYPPFRPPIRPPIFPPIRPPFRPP LRFP 155 Bactenecin 5 Ovis aries 176 METQGASLSLGRWSLWLLLLGLVLPSASAQALSYR precursor EAVLRAVGQLNERSSEANLYRLLELDPAPNDEVDP (BAC5) GTRKPVSFTVKETVCPRTTQQPPEECDFKENGLVK QCVGTVTLDPSNDQFDINCNELQSVRFRPPIRRPPI RPPFRPPFRPPVRPPIRPPFRPPFRPPIGPFPGRR 156 Bactenecin 5 Bos taurus 176 METQRASLSLGRCSLWLLLLGLVLPSASAQALSYRE precursor AVLRAVDQFNERSSEANLYRLLELDPTPNDDLDPGT (BAC5) (PR-42) RKPVSFRVKETDCPRTSQQPLEQCDFKENGLVKQC VGTVTLDPSNDQFDINCNELQSVRFRPPIRRPPIRP PFYPPFRPPIRPPIFPPIRPPFRPPLGPFPGRR 157 Bactenecin 5 Capra 176 METQGASLSLGRWSLWLLLLGLVVPLASAQALSYR precursor hircus EAVLRAVGQLNERSSEANLYRLLELDPAPNDEVDP (CHBAC5) GTRKPVSFTVKETVCPRTTQQPPEECDFKENGLVK QCVGTVTLDPSNDQFDINCNELQSVRFRPPIRRPPI RPPFNPPFRPPVRPPFRPPFRPPFRPPIGPFPGRR 158 bactenecin 7 Bos taurus 59 RRIRPRPPRLPRPRPRPLPFPRPGPRPIPRPLPFPR PGPRPIPRPLPFPRPGPRPIPRP 159 Bactenecin 7 Ovis aries 190 METQMASPSLGRCSLWLLLLGLLLPSASAQALSYR precursor EAVLRAVGQLNEKSSEVNLYRLLELDPPPKDAEDQ (BAC7) GARKPVSFRVKETVCPRMSQQPPEQCDFKENGLV KQCVGTVSLDTSNDEFDLNCNELQSVRRLRPRRPR LPRPRPRPRPRPRSLPLPRPQPRRIPRPILLPWRPP RPIPRPQPQPIPRWL 160 Bactenecin 7 Bos taurus 190 METQRASLSLGRWSLWLLLLGLVLPSASAQALSYR precursor EAVLRAVDRINERSSEANLYRLLELDPPPKDVEDRG (BAC7) (PR-59) ARKPTSFTVKETVCPRTSPQPPEQCDFKENGLVKQ CVGTITLDQSDDLFDLNCNELQSVRRIRPRPPRLPR PRPRPLPFPRPGPRPIPRPLPFPRPGPRPIPRPLPF PRPGPRPIPRPL 161 beta defensin Mus 74 MKISYFLLLILSLGSSQINPVSGDDSIQCFQKNNTCH 39 musculus TNQCPYFQDEIGTCYDRRGKCCQKRLLHIRVPRKK KV 162 Beta defensin 9 Mus 78 MPVTKSYFMTVVVVLILVDETTGGLFGFRSSKRQEP precursor musculus WIACELYQGLCRNACQKYEIQYLSCPKTRKCCLKYP (Hypothetical RKITSF defensin-like structure containing protein) 163 Beta defensin-2 Capra 64 MRLHHLLLALFFLVLSAGSGFTQGIINHRSCYRNKG precursor hircus VCAPARCPRNMRQIGTCHGPPVKCCRKK 164 Beta-defensin 1 Bos taurus 38 DFASCHTNGGICLPNRCPGHMIQIGICFRPRVKCCR (BNDB-1) SW (BNBD-1) 165 Beta-defensin 1 Capra 64 MRLHHLLLVLFFLVLSAGSGFTQGIRSRRSCHRNKG precursor (BD- hircus VCALTRCPRNMRQIGTCFGPPVKCCRKK 1) 166 Beta-defensin 1 Sus scrofa 64 MRLHRLLLVFLLMVLLPVPGLLKNIGNSVSCLRNKG precursor (BD- VCMPGKCAPKMKQIGTCGMPQVKCCKRK 1) (Defensin, beta 1) 167 Beta-defensin 1 Pan 68 MRTSYLLLFTLCLLLSEMASGGNFLTGLGHRSDHYN precursor (BD- troglodytes CVSSGGQCLYSACPIFTKIQGTCYRGKAKCCK 1) (hBD-1) (Defensin, beta 1) 168 Beta-defensin 1 Mus 69 MKTHYFLLVMICFLFSQMEPGVGILTSLGRRTDQYK precursor (BD- musculus CLQHGGFCLRSSCPSNTKLQGTCKPDKPNCCKS 1) (mBD-1) 169 Beta-defensin 1 Rattus 69 MKTHYFLLVMLFFLFSQMELGAGILTSLGRRTDQYR precursor (BD- norvegicus CLQNGGFCLRSSCPSHTKLQGTCKPDKPNCCRS 1) (RBD-1) 170 Beta-defensin 1 Macaca 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHRSDHYN precursor (BD- mulatta CVRSGGQCLYSACPIYTRIQGTCYHGKAKCCK 1) (RhBD-1) (Defensin, beta 1) 171 Beta-defensin 1 Ovis aries 64 MRLHHLLLVLFFVVLSAGSGFTQGVRNRLSCHRNK precursor (BD- GVCVPSRCPRHMRQIGTCRGPPVKCCRKK 1) (sBD1) 172 Beta-defensin Bos taurus 40 QGVRSYLSCWGNRGICLLNRCPGRMRQIGTCLAPR 10 (BNDB-10) VKCCR (BNBD-10) 173 Beta-defensin Bos taurus 38 GPLSCRRNGGVCIPIRCPGPMRQIGTCFGRPVKCC 11 (BNDB-11) RSW (BNBD-11) 174 Beta-defensin Macaca 123 MKLLLLALPILVLLPQVIPAYGGEKKCWNRSGHCRK 118 precursor mulatta QCKDGEAVKETCKNHRACCVPSNEDHRRLPTTSPT (Epididymal PLSDSTPGIIDNILTIRFTTDYFEISSKKDMVEESEAG secretory QGTQTSPPNVHHTS protein 13.6) (ESP13.6) 175 Beta-defensin Bos taurus 38 GPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCC 12 (BNDB-12) RSW (BNBD-12) 176 Beta-defensin Macaca 123 MKSLLFTLAVFMLLAQLVSGNLYVKRCLNDIGICKKT 126 precursor fascicularis CKPEEVRSEHGWVMCGKRKACCVPADKRSAYPSF (Epididymal CVHSKTTKTSTVTARATATTATTATAATPLMISNGLI secretory SLMTTMAATPVSPTT protein 13.2) (ESP13.2) 177 Beta-defensin Bos taurus 42 SGISGPLSCGRNGGVCIPIRCPVPMRQIGTCFGRPV 13 (BNDB-13) KCCRSW (BNBD-13) 178 Beta-defensin 2 Macaca 64 MRVLYLLFSFLFIFLMPLPGVFGGIGDPVTCLKNGAI mulatta CHPVFCPRRYKQIGTCGLPGTKCCKKP 179 Beta-defensin 2 Bos taurus 40 VRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRIKC (BNDB-2) CRSW (BNBD-2) 180 Beta-defensin 2 Mus 71 MRTLCSLLLICCLLFSYTTPAVGSLKSIGYEAELDHC precursor (BD- musculus HTNGGYCVRAICPPSARRPGSCFPEKNPCCKYMK 2) (mBD-2) 181 Beta-defensin 2 Rattus 63 MRIHYLLFSFLLVLLSPLSAFTQSINNPITCLTKGGVC precursor (BD- norvegicus WGPCTGGFRQIGTCGLPRVRCCKKK 2) (RBD-2) 182 Beta-defensin 2 Ovis aries 64 MRLHHLLLVLFFVVLSAGSGFTHGVTDSLSCRWKK precursor (BD- GICVLTRCPGTMRQIGTCFGPPVKCCRLK 2) (sBD2) 183 Beta-defensin 3 Mus 63 MRIHYLLFAFLLVLLSPPAAFSKKINNPVSCLRKGGR precursor (BD- musculus CWNRCIGNTRQIGSCGVPFLKCCKRK 3) (mBD-3) 184 Beta-defensin 3 Bos taurus 57 LALLFLVLSAGSGFTQGVRNHVTCRINRGFCVPIRC precursor PGRTRQIGTCFGPRIKCCRSW (BNDB-3) (BNBD-3) (Fragment) 185 Beta-defensin 4 Mus 63 MRIHYLLFTFLLVLLSPLAAFTQIINNPITCMTNGAIC precursor (BD- musculus WGPCPTAFRQIGNCGHFKVRCCKIR 4) (mBD-4) 186 Beta-defensin 4 Bos taurus 63 MRLHHLLLAVLFLVLSAGSGFTQRVRNPQSCRWNM precursor GVCIPFLCRVGMRQIGTCFGPRVPCCRR (BNDB-4) (BNBD-4) 187 beta-defensin 4 Mus 63 MRIHYLLFTFLPVLLSPLAAFTQIINNPITCMTNGAIC variant musculus WGPCPTAFRQIGNCGHFKVRCCKIR 188 Beta-defensin 5 Bos taurus 64 MRLHHLLLVLLFLVLSAGSGFTQVVRNPQSCRWNM precursor GVCIPISCPGNMRQIGTCFGPRVPCCRRW (BNDB-5) (BNBD-5) 189 Beta-defensin 6 Mus 63 MKIHYLLFAFILVMLSPLAAFSQLINSPVTCMSYGGS musculus CQRSCNGGFRLGGHCGHPKIRCCRRK 190 Beta-defensin 6 Bos taurus 42 QGVRNHVTCRIYGGFCVPIRCPGRTRQIGTCFGRP (BNDB-6) VKCCRRW (BNBD-6) 191 Beta-Defensin 7 Mus 37 NSKRACYREGGECLQRCIGLFHKIGTCNFRFKCCKFQ musculus 192 Beta-defensin 7 Bos taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPRI (BNDB-7) KCCR (BNBD-7) 193 Beta-defensin 7 Mus 71 MRIHYVLFAFLLVLLSPFAAFSQDINSKRACYREGGE precursor musculus CLQRCIGLFHKIGTCNFRFKCCKFQIPEKKTKIL 194 Beta-Defensin 8 Mus 35 NEPVSCIRNGGICQYRCIGLRHKIGTCGSPFKCCK musculus 195 Beta-defensin 8 Mus 60 MRIHYLLFTFLLVLLSPLAAFSQKINEPVSCIRNGGIC (Beta-defensin musculus QYRCIGLRHKIGTCGSPFKCCK 6) 196 Beta-defensin 8 Bos taurus 38 VRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPQIKC (BNDB-8) CR (BNBD-8) 197 Beta-defensin 9 Bos taurus 55 LALLFLVLSAGSGFTQGVRNFVTCRINRGFCVPIRC precursor PGHRRQIGTCLAPQIKCCR (BNDB-9) (BNBD-9) (Fragment) 198 Beta-defensin Bos taurus 53 LALLFLVLSAGSGISGPLSCRRKGGICILIRCPGPMR C7 precursor QIGTCFGRPVKCCRSW (BBD(C7)) (Fragment) 199 Beta-defensin Gallus 80 MRIVYLLIPFFLLFLQGAAGTATQCRIRGGFCRVGSC prepropeptide gallus RFPHIAIGKCATFISCCGRAYEVDALNSVRTSPWLLA PGNNPH 200 Beta-defensin Meleagris 59 MRIVYLLFPFFLLFLQSAAGTPIQCRIRGGFCRFGSC prepropeptide gallopavo RFPHIAIAKCATFIPCCGSIWG 201 Beta-defensin-1 Equus 64 MRILHFLLAFLIVFLLPVPGFTAGIETSFSCSQNGGF caballus CISPKCLPGSKQIGTCILPGSKCCRKK 202 Beta-defensin- Mus 85 MKNLPSNMALSREVFYFGFALFFIVVELPSGSWAGL 12 musculus EYSQSFPGGEIAVCETCRLGRGKCRRTCIESEKIAG (Hypothetical WCKLNFFCCRERI defensin-like structure containing protein) 203 Beta-defensin-2 Pan 64 MRVLYLLFSFLFIFLMPLPGVFGGISDPVTCLKSGAI troglodytes CHPVFCPRRYKQIGTCGLPGTKCCKKP 204 beta-defensin-3 Bos taurus 42 QGVRNHVTCRINRGFCVPIRCPGRTRQIGTCFGPRI KCCRSW 205 Beta-defensin-3 Pan 64 MRIHYLLFALLFLFLVPVPGHGGIINTLQKYYCRVRG (Fragment) troglodytes GRCAVLTCLPKEEQIGKCSTRGRKCCR 206 beta-defensin-4 Bos taurus 41 QRVRNPQSCRWNMGVCIPFLCRVGMRQIGTCFGP RVPCCRR 207 beta-defensin-5 Bos taurus 40 QVVRNPQSCRWNMGVCIPISCPGNMRQIGTCFGP RVPCCR 208 beta-defensin-9 Bos taurus 40 QGVRNFVTCRINRGFCVPIRCPGHRRQIGTCLGPQI KCCR 209 Beta-defensin- Canis 65 MKAFLLTLAALVLLSQVTSGSAEKCWNLRGSCREK like peptide 1 familiaris CIKNEKLYIFCTSGKLCCLKPKFQPNMLQR 210 Beta-defensin- Canis 69 MKAFLLTLAALVLLSQVTSGSAEECWNLRGSCREK like peptide 2 familiaris CIKNEKLYIFCTSGKLCCLKPKFQPNMLQRSVQF 211 Beta-defensin- Canis 99 MKAFLLTLAALVLLSQVTSGSAEKCWNLRGSCREK like peptide 3 familiaris CIKNEKLYIFCTSGKLCCLKPKFQPNMLQRNRKDNP KICLELQKILNIQSNLDKEEQSWKHCTS 212 Big defensin Tachypleus 79 NPLIPAIYIGATVGPSVWAYLVALVGAAAVTAANIRR tridentatus ASSDNHSCAGNRGWCRSKCFRHEYVDTYYSAVCG RYFCCRSR 213 bombinin H Bombina 20 IIGPVLGMVGSALGGLLKKI Met-8 variegata 214 Bombinin Bombina 21 IIGPVLGMVGSALGGLLKKIG H1/H3 variegata 215 Bombinin H4 Bombina 21 LIGPVLGLVGSALGGLLKKIG variegata 216 Bombinin H5 Bombina 21 IIGPVLGLVGSALGGLLKKIG variegata 217 Bombinin-like Bombina 27 GIGSAILSAGKSALKGLAKGLAEHFAN peptide 2 (BLP- orientalis 2) 218 Bombinin-like Bombina 25 GIGAAILSAGKSIIKGLANGLAEHF peptide 4 (BLP- orientalis 4) 219 Bombinin-like Bombina 144 MNFKYIVAVSFLIASTYARSVKNDEQSLSQRDVLEE peptide 7, BPL- orientalis ESLREIRGIGGALLSAGKSALKGLAKGLAEHFANGK 7 precursor RTAEEHEVMKRLEAVMRDLDSLDYPEEASEMETRS FNQEEIANLFTKKEKRILGPVLDLVGRALRGLLKKIG 220 Bombinin-like Bombina 204 MNFKYIVAVSILIASAYARSEENDIQSLSQRDVLEEE peptides 1 orientalis SLREIRGIGASILSAGKSALKGLAKGLAEHFANGKRT precursor AEDHEVMKRLEAAIQSLSQRDVLEEESLREIRGIGA [Contains: SILSAGKSALKGLAKGLAEHFANGKRTAEEHEVMKR Acidic peptide LEAVMRDLDSLDYPEEASEMETRSFNQEEIANLYTK 1; Bombinin-like KEKRILGPILGLVSNALGGLLG peptide 1 (BLP- 1); Octapeptide 1; Acidic peptide 2; Octapeptide 2; Acidic peptide 3; GH-1 peptide] 221 Bombinin-like Bombina 137 MNFKYIVAVSILIASAYARSEENDIQSLSQRDVLEEE peptides 1 variegata SLREIRGIGGALLSAAKVGLKGLAKGLAEHFANGKR precursor TAEEREVMKRLEAAMRDLDSFEHPEEASEKETRGF [Contains: NQEEKEKRIIGPVLGLVGSALGGLLKKIG Acidic peptide 1-1; Bombinin- like peptide 1 (BLP-1); Octapeptide 1; Acidic peptide 1-2; Bombinin H] 222 Bombinin-like Bombina 137 MNFKYIVAVSILIASAYARREENNIQSLSQRDVLEEE peptides 2 variegata SLREIRGIGASILSAGKSALKGFAKGLAEHFANGKRT precursor AEDHEMMKRLEAAVRDLDSLEHPEEASEKETRGFN [Contains: QEEKEKRIIGPVLGLVGSALGGLLKKIG Acidic peptide 2-1; Bombinin- like peptide 2 (BLP-2); Octapeptide 2; Acidic peptide 2-2; Bombinin H2] 223 Bombinin-like Bombina 200 MNFKYIVAVSILIASAYARSEENDIQSLSQRDVLEEE peptides 3 orientalis SLREIRGIGAAILSAGKSALKGLAKGLAEHFGKRTAE precursor DHEVMKRLEAAIHSLSQRDVLEEESLREIRGIGAAIL [Contains: SAGKSALKGLAKGLAEHFGKRTAEEHEMMKRLEAV Acidic peptide MRDLDSLDYPEEASEMETRSFNQEEIANLYTKKEKR 1; Bombinin-like ILGPILGLVSNALGGLLG peptide 3 (BLP- 3); Octapeptide 1; Acidic peptide 2; Octapeptide 2; Acidic peptide 3; GH-1 peptide] 224 Bovine Bos taurus 38 APLSCGRNGGVCIPIRCPVPMRQIGTCFGRPVKCC Neutrophil RSW Beta-Defensin 12 225 Brevinin-1 Rana 24 FLPVLAGIAAKVVPALFCKITKKC brevipoda 226 Brevinin-1BA Rana 24 FLPFIAGMAAKFLPKIFCAISKKC berlandieri 227 Brevinin-1BB Rana 24 FLPAIAGMAAKFLPKIFCAISKKC berlandieri 228 Brevinin-1BC Rana 24 FLPFIAGVAAKFLPKIFCAISKKC berlandieri 229 Brevinin-1BD Rana 24 FLPAIAGVAAKFLPKIFCAISKKC berlandieri 230 Brevinin-1BE Rana 24 FLPAIVGAAAKFLPKIFCVISKKC berlandieri 231 Brevinin-1BF Rana 24 FLPFIAGMAANFLPKIFCAISKKC berlandieri 232 Brevinin-1E Rana 71 MFTLKKSMLLLFFLGTINLSLCEEERDADEEERRDN precursor esculenta PDESEVEVEKRFLPLLAGLAANFLPKIFCKITRKC 233 Brevinin-1Ea Rana 24 FLPAIFRMAAKVVPTIICSITKKC esculenta 234 brevinin-1Eb Rana 24 VIPFVASVAAEMMQHVYCAASRKC esculenta 235 Brevinin-1Eb Rana 23 VIPFVASVAAEMQHVYCAASRKC esculenta 236 Brevinin-1LA Rana 24 FLPMLAGLAASMVPKLVCLITKKC luteiventris 237 Brevinin-1LB Rana 24 FLPMLAGLAASMVPKFVCLITKKC luteiventris 238 Brevinin-1PA Rana 24 FLPIIAGVAAKVFPKIFCAISKKC pipiens 239 Brevinin-1PB Rana 24 FLPIIAGIAAKVFPKIFCAISKKC pipiens 240 Brevinin-1PC Rana 24 FLPIIASVAAKVFSKIFCAISKKC pipiens 241 Brevinin-1PD Rana 24 FLPIIASVAANVFSKIFCAISKKC pipiens 242 Brevinin-1PE Rana 24 FLPIIASVAAKVFPKIFCAISKKC pipiens 243 Brevinin-1Sa Rana 24 FLPAIVGAAGQFLPKIFCAISKKC sphenocephala 244 Brevinin-1Sb Rana 24 FLPAIVGAAGKFLPKIFCAISKKC sphenocephala 245 Brevinin-1Sc Rana 24 FFPIVAGVAGQVLKKIYCTISKKC sphenocephala 246 Brevinin-1SY Rana 24 FLPVVAGLAAKVLPSIICAVTKKC sylvatica 247 Brevinin-1T Rana 20 VNPIILGVLPKFVCLITKKC temporaria 248 Brevinin-1TA Rana 17 FITLLLRKFICSITKKC temporaria 249 Brevinin-2 Rana 33 GLLDSLKGFAATAGKGVLQSLLSTASCKLAKTC brevipoda 250 Brevinin-2E Rana 33 GIMDTLKNLAKTAGKGALQSLLNKASCKLSGQC esculenta 251 Brevinin-2Ea Rana 33 GILDTLKNLAISAAKGAAQGLVNKASCKLSGQC esculenta 252 Brevinin-2Eb Rana 33 GILDTLKNLAKTAGKGALQGLVKMASCKLSGQC esculenta 253 Brevinin-2Ec Rana 34 GILLDKLKNFAKTAGKGVLQSLLNTASCKLSGQC esculenta 254 Brevinin-2Ed Rana 29 GILDSLKNLAKNAGQILLNKASCKLSGQC esculenta 255 Brevinin-2Ee Rana 29 GIFDKLKNFAKGVAQSLLNKASCKLSGQC esculenta 256 Brevinin-2Ef Rana 74 MFTMKKSLLLIFFLGTISLSLCQEERNADDDDGEMT precursor esculenta EEEKRGIMDTLKNLAKTAGKGALQSLVKMASCKLS GQC 257 Brevinin-2T Rana 33 GLLSGLKKVGKHVAKNVAVSLMDSLKCKISGDC temporaria 258 Brevinin-2Tb Rana 74 MFTMKKSLLLFFFLGTISLSLCQEERNADEDDGEMT precursor temporaria EEEKRGILDTLKHLAKTAGKGALQSLLNHASCKLSG QC 259 Brevinin-2TC Rana 29 GLWETIKNFGKKFTLNILHKLKCKIGGGC temporaria 260 Brevinin-2TD Rana 29 GLWETIKNFGKKFTLNILHNLKCKIGGGC temporaria 261 buforin I Bufo 129 MSGRGKQGGKVRAKAKTRSSRAGLQFPVGRVHRL gargarizans LRKGNYAQRVGAGAPVYLAAVLEYLTAEILELAGNA ARDNKKTRIIPRHLQLAVRNDEELNKLLGGVTIAQG GVLPNIQAVLLPKTESSKPAKSK 262 Buthinin Androctonus 34 SIVPIRCRSNRDCRRFCGFRGGRCTYARQCLCGY australis 263 Caeridin Litoria 13 MGLLDGLLGTLGL 1.1/1.2/1.3 chloris 264 Caeridin Litoria 12 GLLDGLLGTLGL 1.1/1.2/1.3 xanthomera 265 Caeridin 1.4 Litoria 13 MGLLDGLLGGLGL chloris 266 Caeridin 1.4 Litoria 12 GLLDGLLGGLGL xanthomera 267 Caerin 1.1 Litoria 26 MGLLSVLGSVAKHVLPHVVPVIAEHL caerulea 268 Caerin 1.1 Litoria 25 GLLSVLGSVAKHVLPHVVPVIAEHL splendida 269 Caerin 1.6 Litoria 25 MGLFSVLGAVAKHVLPHVVPVIAEK chloris 270 Caerin 1.6 Litoria 24 GLFSVLGAVAKHVLPHVVPVIAEK xanthomera 271 Caerin 1.7 Litoria 25 MGLFKVLGSVAKHLLPHVAPVIAEK chloris 272 Caerin 1.7 Litoria 24 GLFKVLGSVAKHLLPHVAPVIAEK xanthomera 273 Caerulein Litoria 10 QQDYTGWMDF xanthomera 274 cathelin related Mus 172 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPSYRDA antimicrobial musculus VLRAVDDFNQQSLDTNLYRLLDLDPEPQGDEDPDT peptide PKSVRFRVKETVCGKAERQLPEQCAFKEQGVVKQ CMGAVTLNPAADSFDISCNEPGAQPFRFKKISRLAG LLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPE 275 Cathelin-related Mus 173 MQFQRDVPSLWLWRSLSLLLLLGLGFSQTPSYRDA antimicrobial musculus VLRAVDDFNQQSLDTNLYRLLDLDPEPQGDEDPDT peptide PKSVRFRVKETVCGKAERQLPEQCAFKEQGVVKQ precursor CMGAVTLNPAADSFDISCNEPGAQPFRFKKISRLAG (Cramp) LLRKGGEKIGEKLKKIGQKIKNFFQKLVPQPEQ (Cathelin-like protein) (CLP) 276 Cathelin-related Ovis aries 160 METQRASLSLGRCSLWLLLLGLALPSASAQVLSYRE peptide SC5 AVLRAADQLNEKSSEANLYRLLELDPPPKQDDENS precursor 1 NIPKPVSFRVKETVCPRTSQQPAEQCDFKENGLLKE (Antibacterial CVGTVTLDQVRNNFDITCAEPQSVRGLRRLGRKIAH peptide SMAP- GVKKYGPTVLRIIRIAG 29) (Myeloid antibacterial peptide SMAP- 29) 277 Cathelin-related Ovis aries 160 METQRASLSLGRRSLWLLLLGLVLASASAQALSYRE peptide SC5 AVLRAVDQLNEKSSEANLYRLLELDPPPKQDDENS precursor 2 NIPKPVSFRVKETVCPRTSQQPAEQCDFKENGLLKE (Antibacterial CVGTVTLDQVGNNFDITCAEPQSVRGLRRLGRKIAH peptide SMAP- GVKKYGPTVLRIIRIAG 29) (Myeloid antibacterial peptide SMAP- 29) 278 cathelin-related Ovis aries 160 METQRAGLSLGRRSLWLLLLGLVLASASAQALSYR protein 1 EAVLRAVDQLNEKSSEANLYRLLELDPPPKQDDEN precursor SNIPKPVSFRVKETVCPRTSQQPAEQCDFKENGLLK ECVGTVTLDQVGNNFDITCAEPQSVRGLRRLGRKIA HGVKKYGPTVLRIIRIAG 279 cathelin-related Ovis aries 152 SLGRCSLWLLLLGLALPSASAQVLSYREAVLRAADQ protein 2 LNEKSSEANLYRLLELDPPPKQDDENSNIPKPVSFR precursor VKETVCPRTSQQPAEQCDFKENGLLKECVGTVTLD QVRNNFDITCAEPQSVRGLRRLGRKIAHGVKKYGP TVLRIIRIAG 280 Cecropin Bombyx 35 RWKIFKKIEKVGQNIRDGIVKAGPAVAVVGQAATI (Antibacterial mori peptide CM-IV) 281 Cecropin 1 Ceratitis 63 MNFNKVFILVAIVIAIFAGQTEAGWLKKIGKKIERVGQ precursor capitata HTRDATIQTIAVAQQAANVAATARG 282 Cecropin 1 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKIERIGQ precursor virilis HTRDATIQGLGIAQQAANVAATARG 283 Cecropin 2 Ceratitis 63 MNFNKVLVLLAVIFAVFAGQTEAGWLKKIGKKIERVG precursor capitata QHTRDATIQTIGVAQQAANVAATLKG 284 Cecropin 2 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKIERVGQ precursor virilis HTRDATIQGLGIAQQAANVAATARG 285 Cecropin 3 Drosophila 63 MNFYKVFIFVALILAISLGQSEAGWLKKIGKKIERIGQ precursor virilis HTRDATIQGVGIAQQAANVAATARG 286 Cecropin A Aedes 59 MNFTKLFLLIAVAVLLLTGQSEAGGLKKLGKKLEGA precursor aegypti GKRVFNAAEKALPVVAGAKALRK 287 Cecropin A Bombyx 63 MNFVRILSFVFALVLALGAVSAAPEPRWKLFKKIEKV precursor mori GRNVRDGLIKAGPAIAVIGQAKSLGK 288 Cecropin A Trichoplusia 62 MNLVKILFCVFACLVFTVTAVPEPRWKFFKKIEKVG precursor ni QNIRDGIIKAGPAVAVVGQAASITGK 289 Cecropin A Hyalophora 64 MNFSRIFFFVFACLTALAMVNAAPEPKWKLFKKIEKV precursor cecropia GQNIRDGIIKAGPAVAVVGQATQIAKG (Cecropin C) 290 Cecropin A Spodoptera 57 IFFFVFACLLALSAVSAAPEPRWKVFKKIEKVGRNVR precursor litura DGIIKAGPAIGVLGQAKALG (Fragment) 291 Cecropin A1/A2 Drosophila 63 MNFYNIFVFVALILAITIGQSEAGWLKKIGKKIERVGQ precursor melanogaster HTRDATIQGLGIAQQAANVAATARG 292 Cecropin B Antheraea 35 KWKIFKKIEKVGRNIRNGIIKAGPAVAVLGEAKAL pernyi 293 Cecropin B Drosophila 63 MNFNKIFVFVALILAISLGNSEAGWLRKLGKKIERIGQ precursor melanogaster HTRDASIQVLGIAQQAANVAATARG 294 Cecropin B Spodoptera 58 ILSFVFACLLALSAVSAAPEPRWKVFKKIEKMGRNIR precursor litura DGIVKAGPAIEVLGSAKALGK (Fragment) 295 Cecropin B Hyalophora 62 MNFSRIFFFVFALVLALSTVSAAPEPKWKVFKKIEKM precursor cecropia GRNIRNGIVKAGPAIAVLGEAKALG (Immune protein P9) 296 Cecropin B Bombyx 63 MNFAKILSFVFALVLALSMTSAAPEPRWKIFKKIEKM precursor mori GRNIRDGIVKAGPAIEVLGSAKAIGK (Lepidopteran A and B) 297 Cecropin C Drosophila 63 MNFNKIFVFVALILAISLGQSEAGWLKKLGKRIERIGQ precursor erecta HTRDATIQGLGIAQQAANVAATARG 298 Cecropin C Drosophila 63 MNFYKIFVFVALILAISIGQSEAGWLKKLGKRIERIGQ precursor mauritiana HTRDATIQGLGIAQQAANVAATARG 299 Cecropin D Bombyx 61 MKFSKIFVFVFAIVFATASVSAAPGNFFKDLEKMGQ precursor mori RVRDAVISAAPAVDTLAKAKALGQG 300 Cecropin D Hyalophora 62 MNFTKILFFVVACVFAMRTVSAAPWNPFKELEKVG precursor cecropia QRVRDAVISAGPAVATVAQATALAKGK 301 Cecropin P1 Sus scrofa 31 SWLSKTAKKLENSAKKRISEGIAIAIQGGPR 302 ceratotoxin A Ceratitis 29 SIGSALKKALPVAKKIGKIALPIAKAALP capitata 303 Ceratotoxin A Ceratitis 71 MANLKAVFLICIVAFIALQCVVAEPAAEDSVVVKRSIG precursor 1 capitata SALKKALPVAKKIGKIALPIAKAALPVAAGLVG 304 Ceratotoxin A Ceratitis 71 MANLKAVFLICIVAFIAFQCVVAEPAAEDSIVVKRSIG precursor 2 capitata SALKKALPVAKKIGKIALPIAKAALPVAAGLVG 305 Ceratotoxin B Ceratitis 29 SIGSAFKKALPVAKKIGKAALPIAKAALP capitata 306 Ceratotoxin C Ceratitis 67 MANIKAVFLICIVAFIAFHCVVAEPTAEDSVVVKRSLG precursor capitata GVISGAKKVAKVAIPIGKAVLPVVAKLVG 307 Ceratotoxin D Ceratitis 71 MANLKAVFLICILAFIAFHCVVGAPTAEDSIVVKRSIG precursor capitata TAVKKAVPIAKKVGKVAIPIAKAVLSVVGQLVG 308 Chlamysin Chlamys 137 MMYFVLFCLLAAGTTYGSHNFATGIVPHSCLECICK precursor islandica TESGCRAIGCKFDVYSDSCGYFQLKQAYWEDCGR PGGSLTSCADDIHCSSQCVQHYMSRYIGHTSCSRT CESYARLHNGGPHGCEHGSTLGYWGHVQGHGC 309 Chromogranin Bos taurus 449 MRSAAVLALLLCAGQVIALPVNSPMNKGDTEVMKCI A precursor VEVISDTLSKPSPMPVSKECFETLRGDERILSILRHQ (CgA) (Pituitary NLLKELQDLALQGAKERTHQQKKHSSYEDELSEVL secretory EKPNDQAEPKEVTEEVSSKDAAEKRDDFKEVEKSD protein I) (SP-I) EDSDGDRPQASPGLGPGPKVEEDNQAPGEEEEAP [Contains: SNAHPLASLPSPKYPGPQAKEDSEGPSQGPASREK Vasostatin-1; GLSAEQGRQTEREEEEEKWEEAEAREKAVPEEES Chromostatin; PPTAAFKPPPSLGNKETQRAAPGWPEDGAGKMGA Chromacin; EEAKPPEGKGEWAHSRQEEEEMARAPQVLFRGGK Pancreastatin; SGEPEQEEQLSKEWEDAKRWSKMDQLAKELTAEK WE-14; RLEGEEEEEEDPDRSMRLSFRARGYGFRGPGLQL Catestatin] RRGWRPNSREDSVEAGLPLQVRGYPEEKKEEEGS ANRRPEDQELESLSAIEAELEKVAHQLEELRRG 310 chromogranin B Bos taurus 170 MPVDIRNHNEEVVTHLRDPADTSEAPGLSAGEPPG SQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEV GSEERLSEGPQRNQTPAKKSSQEGNPPLEEESHV GTGALEEGAERLPGELRNYLDYGEEKGEESAEFPD FYDSEEQMSPQHTAEDLELQKIAEKFSGTRRG 311 Chrysophsin-1 Pagrus 25 FFGWLIKGAIHAGKAIHGLIHRRRH major 312 Chrysophsin-2 Pagrus 25 FFGWLIRGAIHAGKAIHGLIHRRRH major 313 Chrysophsin-3 Pagrus 20 FIGLLISAGKAIHDLIRRRH major 314 Cicadin Cicada 55 NEYHGFVDKANNENKRKKQQGRDDFVVKPNNFAN (Fragment) flammata RRRKDDYNENYYDDVDAADVV 315 Citropin 1.1 Litoria 16 GLFDVIKKVASVIGGL [Contains: citropa Citropin 1.1.1; Citropin 1.1.2] 316 Citropin 1.1.3 Litoria 18 GLFDVIKKVASVIGLASP citropa 317 Citropin 1.1.4 Litoria 18 GLFDVIKKVASVIGLASQ citropa 318 Citropin 1.2 Litoria 16 GLFDIIKKVASVVGGL [Contains: citropa Citropin 1.2.1; Citropin 1.2.2; Citropin 1.2.3] 319 Citropin 1.2.4 Litoria 18 GLFDIIKKVASVVGLASP citropa 320 Citropin 1.2.5 Litoria 18 GLFDIIKKVASVVGLASQ citropa 321 Citropin 1.3 Litoria 16 GLFDIIKKVASVIGGL citropa 322 Citropin 2.1.3 Litoria 26 GLIGSIGKALGGLLVDVLKPKLQAAS [Contains: citropa Citropin 2.1.2; Citropin 2.1.1; Citropin 2.1] 323 Citropin 3.1.2 Litoria 24 DLFQVIKEKLKELTGGVIEGIQGV [Contains: citropa Citropin 3.1.1; Citropin 3.1] 324 Clavanin A Styela 80 MKTTILILLILGLGINAKSLEERKSEEEKVFQFLGKIIH precursor clava HVGNFVHGFSHVFGDDQQDNGKFYGHYAEDNGKH WYDTGDQ 325 Clavanin B Styela 23 VFQFLGRIIHHVGNFVHGFSHVF clava 326 Clavanin C Styela 80 MKTTILILLILGLGINAKSLEERKSEEEKVFHLLGKIIH precursor clava HVGNFVYGFSHVFGDDQQDNGKFYGHYAEDNGKH WYDTGDQ 327 Clavanin D Styela 80 MKTTILILLILGLGINAKSLEERKSEEEKAFKLLGRIIH precursor clava HVGNFVYGFSHVFGDDQQDNGKFYGHYAEDNGKH WYDTGDQ 328 Clavanin E Styela 80 MKTTILILLILGLGINAKSLEERKSEEEKLFKLLGKIIHH precursor clava VGNFVHGFSHVFGDDQQDNGKFYGYYAEDNGKH WYDTGDQ 329 Coleoptericin Zophobas 74 SLQGGAPNFPQPSQQNGGWQVSPDLGRDDKGNT atratus RGQIEIQNKGKDHDFNAGWGKVIRGPNKAKPTWHV GGTYRR 330 Corticostatin I Oryctolagus 93 MRTLILLAAILLAALQAQAELFSVNVDEVLDQQQPGS precursor (CS-I) cuniculus DQDLVIHLTGEESSALQVPDTKGICACRRRFCPNSE (Neutrophil RFSGYCRVNGARYVRCCSRR antibiotic peptide NP-3A) (Microbicidal peptide NP-3A) (Antiadrenocorticotropin peptide I) 331 Corticostatin II Oryctolagus 34 GRCVCRKQLLCSYRERRIGDCKIRGVRFPFCCPR (CS-II) cuniculus (Neutrophil antibiotic peptide NP-3B) (Microbicidal peptide NP-3B) (Antiadrenocorticotropin peptide II) 332 Corticostatin III Oryctolagus 95 MRTLALLAAILLVALQAQAEHVSVSIDEVVDQQPPQ precursor (CS- cuniculus AEDQDVAIYVKEHESSALEALGVKAGVVCACRRAL III) CLPRERRAGFCRIRGRIHPLCCRR (Macrophage antibiotic peptide MCP-1) (NP-1) (Antiadrenocorticotropin peptide III) 333 Corticostatin IV Oryctolagus 95 MRTLALLAAILLVALQAQAEHISVSIDEVVDQQPPQA precursor (CS- cuniculus EDQDVAIYVKEHESSALEALGVKAGVVCACRRALCL IV) PLERRAGFCRIRGRIHPLCCRR (Macrophage antibiotic peptide MCP- 2) (NP-2) (Antiadrenocorticotropin peptide IV 334 Corticostatin VI Oryctolagus 34 GICACRRRFCLNFEQFSGYCRVNGARYVRCCSRR (CS-VI) cuniculus (Neutrophil antibiotic peptide NP-6) 335 Corticostatin- Oryctolagus 32 MPCSCKKYCDPWEVIDGSCGLFNSKYICCREK related peptide cuniculus RK-1 336 Crabrolin Vespa 13 FLPLILRKIVTAL crabro 337 cryptdin Mus 23 CKRRERMNGTCRKGHLLYTLCCR musculus 338 cryptdin 12 Mus 35 LRDLVCYCRARGCKGRERMNGTCRKGHLLYMLCCR musculus 339 Cryptdin-1 Mus 35 LRDLVCYCRTRGCKRRERMNXTCRKGHLMYTLCCX (CR1) musculus 340 Cryptdin-1 Mus 93 MKKLVLLFALVLLGFQVQADSIQNTDEETKTEEQPG precursor musculus EEDQAVSVSFGDPEGTSLQEESLRDLVCYCRSRGC (DEFCR) KGRERMNGTCRKGHLLYTLCCR 341 cryptdin-10 Mus 35 LRDLVCYCRKRGCKGRERMNGTCRKGHLLYTLCCR musculus 342 Cryptdin-10 Mus 92 KTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPGE precursor musculus DDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRGC (Fragment) KGRERMNGTCRKGHLLYTMCCR 343 cryptdin-11 Mus 35 LRDLVCYCRSRGCKGRERMNGTCRKGHLLYMLCCR musculus 344 Cryptdin-11 Mus 85 ALVLLAFQVQADPIQNTDEETKTEEQPGEEDQAVSV precursor musculus SFGDPEGTSLQEESLRDLVCYCRSRGCKGRERMN (Fragment) GTCRKGHLLYMLCCR 345 cryptdin-13 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRRGHLMYTLCCR musculus 346 Cryptdin-13 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPG precursor musculus EEDQAVSVSFGDPEGTSLQEESLRDLVCYCRKRGC KRREHMNGTCRRGHLMYTLCCR 347 Cryptdin-14 Mus 85 ALVLLAFQVQADPIQNTDEETKTEEQPGEDDQAVSV precursor musculus SFGDPEGSSLQEESLRDLVCYCRTRGCKRRERMN (Fragment) GTCRKGHLMHTLCCR 348 cryptdin-15 Mus 35 LRDLVCYCRKRGCKRREHINGTCRKGHLLYMLCCR musculus 349 Cryptdin-15 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPG precursor musculus EDDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRG CKRREHINGTCRKGHLLYMLCCR 350 cryptdin-16 Mus 35 LRDLVCYCRSRGCKGRERMNGTCRKGHLMYTLCCR musculus 351 Cryptdin-16 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGE precursor musculus EDQAVSVSFGDPEGTSLQEESLRDLVCYCRSRGCK GRERMNGTCRKGHLMYTLCCR 352 Cryptdin-17 Mus 82 LLAFQVQADPIQNTDEETKTEEQPGEEDQAVSVSF precursor musculus GDPEGTSLQEESLRDLVCYCRKRGCKRREHMNGT (CRYP17) CRKGHLLYTLCCR (Fragment) 353 Cryptdin-2 Mus 35 LRDLVCYCRARGXKGRERMNGTXRKGHLLYMXXXX (CR2) musculus 354 Cryptdin-2 Mus 93 MKPLVLLSALVLLSFQVQADPIQNTDEETKTEEQSG precursor musculus EEDQAVSVSFGDREGASLQEESLRDLVCYCRTRGC KRRERMNGTCRKGHLMYTLCCR 355 Cryptdin-3 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPG precursor musculus EDDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRG CKRRERMNGTCRKGHLMYTLCCR 356 cryptdin-4 Mus 34 LRGLLCYCRKGHCKRGERVRGTCGIRFLYCCPRR musculus 357 Cryptdin-4 Mus 92 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPG precursor musculus EEDQAVSISFGGQEGSALHEKSLRGLLCYCRKGHC KRGERVRGTCGIRFLYCCPRR 358 Cryptdin-5 Mus 93 MKTFVLLSALVLLAFQVQADPIHKTDEETNTEEQPG precursor musculus EEDQAVSISFGGQEGSALHEELSKKLICYCRIRGCK RRERVFGTCRNLFLTFVFCCS 359 Cryptdin-6/12 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGE precursor musculus EDQAVSVSFGDPEGTSLQEESLRDLVCYCRARGCK GRERMNGTCRKGHLLYMLCCR 360 cryptdin-7 Mus 35 LRDLVCYCRTRGCKRREHMNGTCRKGHLMYTLCCR musculus 361 Cryptdin-7 Mus 93 MKTLILLSALVLLAFQVQADPIQNTDEETKTEEQPGE precursor musculus DDQAVSVSFGDPEGSSLQEESLRDLVCYCRTRGCK RREHMNGTCRKGHLMYTLCCR 362 cryptdin-8 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRKGHLMYTLCCR musculus 363 Cryptdin-8 Mus 81 LAFQVQADPIQNTDEETKTEEQPGEDDQAVSVSFG precursor musculus DPEGSSLQEESLRDLVCYCRKRGCKRREHMNGTC (Fragment) RKGHLMYTLCCR 364 cryptdin-9 Mus 35 LRDLVCYCRKRGCKRREHMNGTCRKGHLLYMLCCR musculus 365 Cryptdin-9 Mus 93 MKTLVLLSALVLLAFQVQADPIQNTDEETKTEEQPG precursor musculus EEDQAVSVSFGDPEGSSLQEESLRDLVCYCRKRGC KRREHMNGTCRKGHLLYMLCCR 366 Cryptdin-related Mus 116 MKTLVLLSALVLPCFQVQADPIQNTDEETKTEEQPE protein 1C musculus EEDQAVSVSFGGTEGSALQDVAQRRFPWCRKCRV precursor CQKCQVCQKCPVCPTCPQCPKQPLCEERQNKTAIT (CRS1C) TQAPNTQHKGC 367 Cryptdin-related Mus 91 MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQPG protein 4C-1 musculus EKDQAVSVSFGDPQGSALQDAALGWGRRCPQCPR precursor CPSCPSCPRCPRCPRCKCNPK (CRS4C) 368 Cryptdin-related Mus 91 MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQQG protein 4C-2 musculus EEDQAVSVSFGDPQGSGLQDAALGWGRRCPRCPP precursor CPRCSWCPRCPTCPRCNCNPK (CRS4C) 369 Cryptdin-related Mus 91 MKKLVLLSAFVLLAFQVQADSIQNTDEETKTEEQPG protein 4C-4 musculus EENQAMSVSFGDPEGSALQDAAVGMARPCPPCPS precursor CPSCPWCPMCPRCPSCKCNPK (CRS4C) 370 Cryptdin-related Mus 91 MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTEEQPGE protein 4C-5 musculus ENQAVSISFGDPEGYALQDAAIRRARRCPPCPSCLS precursor CPWCPRCLRCPMCKCNPK (CRS4C) 371 Cyclic Bos taurus 155 METPRASLSLGRWSLWLLLLGLALPSASAQALSYR dodecapeptide EAVLRAVDQLNEQSSEPNIYRLLELDQPPQDDEDP precursor DSPKRVSFRVKETVCSRTTQQPPEQCDFKENGLLK (Bactenecin 1) RCEGTVTLDQVRGNFDITCNNHQSIRITKQPWAPPQ AARLCRIVVIRVCR 372 Cyclic Ovis aries 155 METQRASLSLGRCSLWLLLLGLALPSASAQVLSYRE dodecapeptide AVLRAVDQLNEQSSEPNIYRLLELDQPPQDDEDPD precursor SPKRVSFRVKETVCPRTTQQPPEQCDFKENGLLKR (Bactenecin 1) CEGTVTLDQVRGNFDITCNNHQSIRITKQPWAPPQA ARICRIIFLRVCR 373 DEFB1-like Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHRSDHYN protein aethiops CVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK 374 DEFB1-like Cercopithecus 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHRSDHYI protein erythrogaster CVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK 375 DEFB1-like Gorilla 68 MRTSYLLLFTLCLLLSEIASGGNFLTGLGHRSDHYN protein gorilla CVSSGGQCLYSACPIFTKIQGTCYGGKAKCCK 376 DEFB1-like Hylobates 68 MRTSYLLLFTLCLLLSEMASGDNFLTGLGHRSDHYN protein concolor CVRSGGQCLYSACPIYTKIQGTCYQGKAKCCK 377 DEFB1-like Pan 68 MRTSYLLLFTLCLLLSEMASGGNFLTGLGHRSDHYN protein troglodytes CVSSGGQCLYSACPIFTKIQGTCYGGKAKCCK 378 DEFB1-like Presbytis 68 MRTSYLLLFTLCLLMSEMASGDNFLTGLGHRSDHY protein obscura NCVRSGGQCLYSACPIYTKIQGTCYHGKAKCCK 379 DEFB1-like Saguinus 68 MRTSYLLLFILCLVLCDMDSGDTFLTGLGHRSDHYN protein oedipus CVKGGGQCLYSACPIYTKVQGTCYGGKAKCCK 380 DEFB36 Mus 43 MKLLLLTLAALLLVSQLTPGDAQKCWNLHGKCRHR (Fragment) musculus CSRKESVY 381 Defensin Aeshna 38 GFGCPLDQMQCHRHCQTITGRSGGYCSGPLKLTC cyanea TCYR 382 Defensin Allomyrina 43 VTCDLLSFEAKGFAANHSLCAAHCLAIGRRGGSCE dichotoma RGVCICRR 383 Defensin Anopheles 102 MKCATIVCTIAVVLAATLLNGSVQAAPQEEAALSGG gambiae ANLNTLLDELPEETHHAALENYRAKRATCDLASGFG VGNNLCAAHCIARRYRGGYCNSKAVCVCRN 384 defensin Anopheles 131 NSRVNGATPAKLKLVLLCLPRASSSPQLIMKCATIVC gambiae TIAVVLAATLLNGSVQAAPQEEAALSGGANLNTLLD ELPEETHHAALENYRAKRATCDLASGFGVGSSLCA AHCIARRYRGGYCNSKAVCVCRN 385 Defensin Bombus 51 VTCDLLSIKGVAEHSACAANCLSMGKAGGRCENGI pascuorum CLCRKTTFKELWDKRF 386 Defensin Branchiostoma 117 MEKKTAYCLLFLVLLVPYTALGAVLKRAPAKKEKRA belcheri VPLAVPLVYWGASVSPAVWNWLLVTFGAAAVAAAA VTVSDNDSHSCANNRGWCRSRCFSHEYIDSWHSD VCGSYDCCRPRY 387 Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPEDHVLV melanogaster HEDAHQEVLQHSRQKRATCDLLSKWNWNHTACAG HCIAKGFKGGYCNDKAVCVCRN 388 Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPEDHVLV melanogaster HEDANQEVLQHSRQKRATCDLLSKWNWNHTACAG HCIAKGFKGGYCNDKAVCVCRN 389 Defensin Drosophila 92 MKFFVLVAIAFALLTCMAQAQPVSDVDPIPEDHVLV melanogaster HEDAHQEVLQHSRQKRATCDLLSKWNWNHTACAG HCIAKGFKGGYCNDKAVCVCRN 390 Defensin Drosophila 92 MKFFVPVAIAFALLACVAQAQPVSDVDPIPEDHVLV melanogaster HDDAHQEVLQHSRQKRATCDLLSKWNWNHTACAG HCIAKGFKGGYCNDKAVCVCRN 391 Defensin Drosophila 92 MKFFVLVAIAFALLACMAQAQPVSDVDPIPEDHALV simulans HEDAHQEVVQHSRQKRATCDLLSKWNWNHTACAG HCIAKGFKGGYCNDKAVCVCRN 392 Defensin Mamestra 98 MLCLADIRIVASCSAAIKSGYGQQPWLAHVAGPYAN brassicae SLFDDVPADSYHAAVEYLRLIPASCYLLDGYAAGRD DGRAHCIAPRNRRLYCASYQVCVCRY 393 Defensin Musca 92 MKYFTMFAFFFVAVCYISQSSASPAPKEEANFVHGA domestica DALKQLEPELHGRYKRATCDLLSGTGVGHSACAAH CLLRGNRGGYCNGKGVCVCRN 394 Defensin Ornithodoros 73 MNKLFIVALVLALAVATMAHEVHDDIEEPSVPRVRR moubata GFGCPFNQYECHAHCSGVPGYKGGYCKGLFKQTC NCY 395 Defensin Ornithodoros 73 MNKLFIVALVLALAVATMAHEVYDDVEEPSVPRVRR moubata GYGCPFNQYQCHSHCSGIRGYKGGYCKGLFKQTC NCY 396 Defensin Palomena 43 ATCDALSFSSKWLTVNHSACAIHCLTKGYKGGRCV prasina NTICNCRN 397 Defensin Phlebotomus 40 ATCDLLSAFGVGHAACAAHCIGHGYRGGYCNSKAV duboscqi CTCRR 398 Defensin Pyrocoelia 55 MKLSVFVLVAVMLVLLCCAMQTEARRRCRSCVPFC rufa GSNERMISTCFSGGVVCCPR 399 Defensin Pyrrhocoris 43 ATCDILSFQSQWVTPNHAGCALHCVIKGYKGGQCKI apterus TVCHCRR 400 Defensin Aedes 57 DELPEETYQAAVENYRRKRATCDLLSGFGVGDSAC (Fragment) albopictus AAHCIARRNRGGYCNAKTVCVC 401 Defensin Apis 57 FEPLEHFENEERADRHRRVTCDLLSFKGQVNDSAC (Fragment) mellifera AANCHSLGKAGGHCEKGVCICR 402 Defensin 1 Stomoxys 39 ATCDLLSGMGVNHSACAAHCVLRGNRGGYCNSKA (Fragment) calcitrans VCVCR 403 Defensin 1 Acalolepta 83 MKFFITFTFVLSLVVLTVYSAPREFAEPEEQDEGHF precursor luxuriosa RVKRFTCDVLSVEAKGVKLNHAACGIHCLFRRRTG GYCNKKRVCICR 404 Defensin 1 Stomoxys 79 MKFLNVVAIALLVVACLAVYSNAAPHEGVKEVAAAK precursor calcitrans PMGITCDLLSLWKVGHAACAAHCLVLGDVGGYCTK EGLCVCKE 405 Defensin 1A Stomoxys 79 MKFLNVVAIALLVVACLSVYSNAAPHEGVKEVAAAK precursor calcitrans PMGITCDLLSLWKVGHAACAAHCLVLGNVGGYCTK EGLCVCKE 406 Defensin 2 Stomoxys 97 MKFFSLFPVIVVVVACLTMRANAAPSAGNEVDHHP precursor calcitrans DYVDGVEALRQLEPELHGRYKRATCDLLSMWNVN HSACAAHCLLLGKSGGRCNDDAVCVCRK 407 Defensin 2A Stomoxys 97 MKFFSLFPVILVVVACLTMRANAAPSAGDEVDHHPD precursor calcitrans YVDGVEALRQLEPELHGRYKRATCDLLSMWNVNH SACAAHCLLLGKSGGRCNDDAVCVCRK 408 Defensin 5 Rattus 93 MKKLVLLSALVLLALQVEAEPTPKTDEGTKTDEQPG precursor (RD- norvegicus KEDQVVSVSIEGQGDPAFQDAVLRDLKCFCRRKSC 5) (Enteric NWGEGIMGICKKRYGSPILCCR defensin) 409 Defensin A Aedes 98 MQSLTVICFLALCTGAITSAYPQEPVLADEARPFANS aegypti LFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA CAAHCIARGNRGGYCNSKKVCVCRN 410 Defensin A Mytilus 37 GFGCPNDYPCHRHCKSIPGRXGGYCGGXHRLRCT edulis CYR 411 Defensin A Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHNDVEEQSVPRVR moubata RGYGCPFNQYQCHSHCSGIRGYKGGYCKGTFKQT CKCY 412 Defensin A Rhodnius 94 MKCILSLVTLFLVAVLVHSHPAEWNTHQQLDDALWE prolixus PAGEVTEEHVARLKRATCDLFSFRSKWVTPNHAAC AAHCLLRGNRGGRCKGTICHCRK 413 defensin A Aedes 37 MKSLTVICFLALCTGAITSAYPQEPVLADEARPFANS isoform 2; aegypti AaDefA2 414 defensin A Aedes 37 MQSLTVICFLALCTGAITSAYPQEPVLADEARPFANS isoform 3; aegypti AaDefA3 415 defensin A Aedes 37 MQPLTVICFLALCTGAITSAYPQEPVLADEARPFANS isoform 4; aegypti AaDefA4 416 Defensin A Aedes 98 MKSITVICFLALCTVAITSAYPQEPVLADEARPFANSL precursor aegypti FDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA (AADEF) CAAHCIARGNRGGYCNSKKVCVCRN 417 defensin A Aedes 98 MQSITVICFLALCTGAITSAYPQEPVLADEARPFANS protein isoform 5 aegypti LFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA CAAHCIARGNRGGYCNSKKVCVCRN 418 defensin alpha-1 Macaca 30 ACYCRIPACLAGERRYGTCFYLGRVWAFCC mulatta 419 defensin alpha-3 Macaca 30 ACYCRIPACLAGERRYGTCFYRRRVWAFCC mulatta 420 defensin alpha-4 Macaca 33 RRTCRCRFGRCFRRESYSGSCNINGRIFSLCCR mulatta 421 defensin alpha-5 Macaca 32 RTCRCRFGRCFRRESYSGSCNINGRIFSLCCR mulatta 422 defensin alpha-6 Macaca 33 RRTCRCRFGRCFRRESYSGSCNINGRISSLCCR mulatta 423 defensin alpha-7 Macaca 32 RTCRCRFGRCFRRESYSGSCNINGRISSLCCR mulatta 424 Defensin B Aedes 40 ATCDLLSGFGVGDSACAAHCIARGNRGGYCNSQKV aegypti CVCRN 425 Defensin B Ornithodoros 73 MNKLFIVALVVALAVATMAQEVHDDVEEQSVPRVR moubata RGYGCPFNQYQCHSHCRGIRGYKGGYCTGRFKQT CKCY 426 Defensin B Rhodnius 94 MKCILSLVTLFLVAVLVHSHPAEWNTQQELDDALWE prolixus PAGEVTEEHVARLKRATCDLLSFSSKWVTPNHAGC AAHCLLRGNRGGHCKGTICHCRK 427 Defensin B Mytilus 35 GFGCPNDYPCHRHCKSIPGRYGGYCGGXHRLRCTC (Fragment) edulis 428 defensin beta Mus 67 MRLHYLLFVFLILFLVPAPGDAFLPKTLRKFFCRIRG 14; beta musculus GRCAVLNCLGKEEQIGRCSNSGRKCCRKKK defensin 14 429 defensin beta Mus 81 MKTFLFLFAVLFFWSQPRMHFFFFDEKCSRINGRCT 34; beta musculus ASCLKNEELVALCWKNLKCCVTVQSCGRSKGNQS defensin 34 DEGSGHMGTRG 430 defensin beta Mus 62 MKFSYFLLLLLSLSNFQNNPVAMLDTIACIENKDTCR 37; beta musculus LKNCPRLHNVVGTCYEGKGKCCHKN defensin 37 431 defensin beta Mus 63 MKISCFLLLILSLYFFQINQAIGPDTKKCVQRKNACH 38; beta musculus YFECPWLYYSVGTCYKGKGKCCQKRY defensin 38 432 defensin beta Mus 73 MKISCFLLMIFFLSCFQINPVAVLDTIKCLQGNNNCHI 40; beta musculus QKCPWFLLQVSTCYKGKGRCCQKRRWFARNHVYHV defensin 40 433 Defensin beta 5 Mus 64 MRIHYLLFAFLLVLLCPLASDFSKTINNPVSCCMIGGI musculus CRYLCKGNILQNGNCGVTSLNCCKRK 434 Defensin C Rhodnius 94 MKCILSLFTLFLVATLVYSYPAEWNSQHQLDDAQW prolixus EPAGELTEEHLSRMKRATCDLLSLTSKWFTPNHAG CAAHCIFLGNRGGRCVGTVCHCRK 435 defensin C Zophobas 43 FTCDVLGFEIAGTKLNSAACGAHCLALGRTGGYCN atratus SKSVCVCR 436 Defensin C Aedes 99 MRTLIVVCFVALCLSAIFTTGSALPGELADDVRPYAN precursor aegypti SLFDELPEESYQAAVENFRLKRATCDLLSGFGVGD SACAAHCIARRNRGGYCNAKKVCVCRN 437 Defensin D Aedes 96 VPTVICFLAMCLVAITGAYPQEPVLADEAQSVANSLF precursor albopictus DELPEESYQAAVENLRLKRATCDLLSGFGVGDSAC (AALDEFD) AAHCIARGNRGGYCNSKKVCVCPI (Fragment) 438 Defensin Heliothis 44 DKLIGSCVWGAVNYTSDCNGECKRRGYKGGHCGS heliomicin virescens FANVNCWCET 439 Defensin Heliothis 44 DKLIGSCVWGAVNYTSDCNGECLLRGYKGGHCGS Heliomicin virescens FANVNCWCET 440 defensin Aedes 98 MKSITVICFLALCTGSITSAYPQDPVLADEARPFANS isoform A1 aegypti LFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA CAAHCIARGNRGGYCNSKKVCVCRN 441 defensin Aedes 98 MKSITVICFLALCTVAITSAYPQEPVLADEARPFANSL isoform B1 aegypti FDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA CAAHCIARGNRGGYCNSQKVCVCRN 442 defensin Aedes 98 MKSITVICFLALCTGSITSAYPQEPVLADEARPFANS isoform B2 aegypti LFDELPEETYQAAVENFRLKRATCDLLSGFGVGDSA CAAHCIARGNRGGYCNSQKVCVCRN 443 defensin Aedes 99 MRTLIVVCFVALCLSAIFTTGSALPEELADDVRSYAN isoform C1 aegypti SLFDELPEESYQAAVENFRLKRATCDLLSGFGVGD SACAAHCIARRNRGGYCNAKKVCVCRN 444 Defensin Mgd-1 Mytilus 39 GFGCPNNYQCHRHCKSIPGRCGGYCGGWHRLRC galloprovincialis TCYRCG 445 Defensin MGD-1 Mytilus 38 GFGCPNNYQCHRHCKSIPGRCGGYCGGXHRLRCT galloprovincialis CYRC 446 Defensin MGD- Mytilus 81 MKAAFVLLVVGLCIMTDVATAGFGCPNNYACHQHC 2 precursor galloprovincialis KSIRGYCGGYCAGWFRLRCTCYRCGGRRDDVEDIF DIYDNVAVERF 447 defensin NP-1 Rattus 32 VTCYCRRTRCGFRERLSGACGYRGRIYRLCCR norvegicus 448 defensin NP-4 Rattus 31 ACYCRIGACVSGERLTGACGLNGRIYRLCCR norvegicus 449 Defensin Anopheles 102 MKCATIVCTIAVVLAATLLNGSVQAAPQEEAALSGG precursor gambiae ANLNTLLDELPEETHHAALENYRAKRATCDLASGFG VGSSLCAAHCIARRYRGGYCNSKAVCVCRN 450 Defensin Drosophila 92 MKFFVLVAIAFALLACVAQAQPVSDVDPIPEDHVLVH precursor melanogaster EDAHQEVLQHSRQKRATCDLLSKWNWNHTACAGH CIAKGFKGGYCNDKAVCVCRN 451 Defensin Oryctes 79 MSRFIVFAFIVAMCIAHSLAAPAPEALEASVIRQKRLT precursor rhinoceros CDLLSFEAKGFAANHSLCAAHCLAIGRKGGACQNG VCVCRR 452 defensin Spodoptera 102 MGVKVINVFLLIAVSACLIHAVAGKPNPRDSSVVEEQ precursor frugiperda SLGPIHNEDLEVKVKPETTTTPEPRIPGRVSCDFEEA NEDAVCQEHCLPKGYTYGICVSHTCSCI 453 Defensin Culex 40 ATCDLLSGFGVNDSACAAHCILRGNRGGYCNGKKV precursor pipiens CVCRN (Fragment) 454 defensin R-2 Rattus 31 VTCSCRTSSCRFGERLSGACRLNGRIYRLCC norvegicus 455 defensin R-5 Rattus 32 VTCYCRSTRCGFRERLSGACGYRGRIYRLCCR norvegicus 456 defensin related Mus 92 MKKLVLLSAFVLLAFQVQADSIQNTDEEIKTEEQPGE cryptdin, related musculus ENQAVSISFGDPEGYALQDAAAIRRARRCPPCPSCL sequence 12 SCPWCPRCLRCPMCKCNPK 457 defensin related Mus 92 MKKLVLLFALVLLAFQVQADSIQNTDEETKTEEQQG cryptdin, related musculus EEDQAVSVSFGDPQGSGLQDAAALGWGRRCPRCP sequence 7 PCPRCSWCPRCPTCPRCNCNPK 458 Defensin Mus 60 MRIHYLLFTFLLVLLSPLAAFSQKINDPVTYIRNGGIC related peptide musculus QYRCIGLRHKIGTCGSPFKCCK 459 Defensin, Zophobas 43 FTCDVLGFEIAGTKLNSAACGAHCLALGRRGGYCN isoforms B and C atratus SKSVCVCR 460 defensin-3 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAAQEQIP mulatta TDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRI PACLAGERRYGTCFYRRRVWAFCC 461 defensin-8 Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAAQEQIP mulatta TDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRI PACLAGERRYGTCFYLRRVWAFCC 462 defensin-like Mus 5 ICSPK gene 1C-1 musculus 463 Defensin-like Ornithorhynchus 42 FVQHRPRDCESINGVCRHKDTVNCREIFLADCYND peptide 1 (DLP- anatinus GQKCCRK 1) 464 Defensin-like Ornithorhynchus 42 IMFFEMQACWSHSGVCRDKSERNCKPMAWTYCEN peptide 2/4 anatinus RNQKCCEY (DLP-2/DLP-4) 465 Defensin-like Ornithorhynchus 38 FEMQYCWSHSGVCRDKSERNNKPMAWTYCENRQ peptide 3 (DLP- anatinus KKCEF 3) 466 Defensin-like Mesobuthus 61 MTYAILIIVSLLPISDGISNVVDKYCSENPLDCNEHCL protein TXKS2 martensii KTKNQIGICHGANGNEKCSCMES 467 Demidefensin 2 Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQ mulatta PGADDQGMAHSFTWPENAALPLSESAKGLRCICTR GFCRLL 468 Demidefensin 3 Macaca 76 MRTLALHTAMLLLVALHAQAEARQARADEAAAQQQ mulatta PGADDQGMAHSFTWPENAALPLSESERGLRCICVL GICRLL 469 Dermaseptin 1 Phyllomedusa 34 ALWKTMLKKLGTMALHAGKAALGAAADTISQGTQ (DS I) sauvagei 470 Dermaseptin BI Phyllomedusa 78 MDILKKSLFLVLFLGLVSLSICEEEKRENEDEEKQDD precursor bicolor EQSEMKRAMWKDVLKKIGTVALHAGKAALGAVADT (Dermaseptin ISQGEQ B1) 471 Dermaseptin Phyllomedusa 77 MAFLKKSLFLVLFLGLVSLSVCEEEKRENEDEEEQE DRG3 bicolor DDEQSEEKRALWKTIIKGAGKMIGSLAKNLLGSQAQ precursor PESEQ (Dermaseptin 3) 472 Dermatoxin Phyllomedusa 77 MAFLKKSLFLVLFLGLVPLSLCESEKREGENEEEQE precursor bicolor DDQSEEKRSLGSFLKGVGTTLASVGKVVSDQFGKL LQAGQG 473 Diptericin A Protophormia 82 DEKPKLILPTPAPPNLPQLVGGGGGNRKDGFGVSV terraenovae DAHQKVWTSDNGGHSIGVSPGYSQHLPGPYGNSR PDYRIGAGYSYNF 474 diptericin B Protophormia 41 DEKPKLVLPSXAPPNLPQLVGGGGGNNKXGXXVSI terraenovae NAAQKV 475 diptericin C Protophormia 39 DEKPKLIXPXXAPXNLXQLVGGGGGNNKKXXGVXV terraenovae XXAQ 476 Diptericin D Protophormia 101 MKLFYLLVICALSLAVMADEKPKLILPTPAPPNLPQL precursor terraenovae VGGGGGNRKDGFGVSVDAHQKVWTSDNGRHSIG VTPGYSQHLGGPYGNSRPDYRIGAGYSYNFG 477 Dolabellanin B2 Dolabella 33 SHQDCYEALHKCMASHSKPFSCSMKFHMCLQQQ auricularia 478 Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPTSHPR melanogaster PIRVRREALAIEDHLTQAAIRPPPILPA 479 Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPTSHPR melanogaster PIRVRREALAIEDHLTQAAIRPPPILPV 480 Drosocin Drosophila 64 MKFTIVFLLLACVFAMGVATPGKPRPYSPRPTSHPR CG10816-PA melanogaster PIRVRREALAIEDHLTQAAIRPPPILPA 481 Drosocin Drosophila 64 MKFTIVFLLLACVFAMAVATPGKPRPYSPRPTSHPR precursor melanogaster PIRVRREALAIEDHLAQAAIRPPPILPA 482 Drosomysin Drosophila 44 DCLSGRYKGPCAVWDNETCRRVCKEEGRSSGHCS melanogaster PSLKCWCEGC 483 Drosomycin Drosophila 70 MMQIKYLFALFAVLMLVVLGANEADADCLSGRYKG precursor melanogaster PCAVWDNETCRRVCKEEGRSSGHCSPSLKCWCE (Cysteine-rich GC peptide) 484 enbocin Bombyx 59 MNFTRIIFFLGVVVFATASGKPWNIFKEIERAVARTR mori DAVISAGPAVATVAAATSVASG 485 Enhancer of Sus scrofa 32 RADTQTYQPYNKDWIKEKIYVLLRRQAQQAGK rudimentary homolog [Contains: Antibacterial peptide 3910] (Fragment) 486 enteric beta Bubalus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNPQSCHRNK defensin bubalis GICVPIRCPGNMRQIGTCLGPPVKCCRRK preproprotein 487 Enteric beta- Bos taurus 64 MRLHHLLLTLLFLVLSAGSGFTQGISNPLSCRLNRGI defensin CVPIRCPGNLRQIGTCFTPSVKCCRWR precursor 488 Eosinophil Cavia 233 MKLLLLLALLLGAVSTRHLKVDTSSLQSLRGEESLA granule major porcellus QDGETAEGATREATAGALMPLPEEEEMEGASGSE basic protein 1 DDPEEEEEEEEEVEFSSELDVSPEDIQCPKEEDTVK precursor FFSRPGYKTRGYVMVGSARTFNEAQWVCQRCYRG (MBP-1) NLASIHSFAFNYQVQCTSAGLNVAQVWIGGQLRGK GRCRRFVWVDRTVWNFAYWARGQPWGGRQRGR CVTLCARGGHWRRSHCGKRRPFVCTY 489 EP2e (ANTI- Mus 69 MKVLLLFAVFFCFVQGNSGDIPPGIRNTVCLMQQGH microbial-like musculus CRLFMCRSGERKGDICSDPWNRCCVPYSVKDRR protein BIN-1B homolog) 490 Esculentin-1 Rana 46 GIFSKLGRKKIKNLLISGLKNVGKEVGMDVVRTGIDIA esculenta GCKIKGEC 491 Esculentin-1A Rana 46 GIFSKLAGKKIKNLLISGLKNVGKEVGMDVVRTGIDIA esculenta GCKIKGEC 492 Esculentin-1B Rana 84 MFTLKKPLLLIVLLGMISLSLCEQERNADEEEGSEIK precursor esculenta RGIFSKLAGKKLKNLLISGLKNVGKEVGMDVVRTGID IAGCKIKGEC 493 Esculentin-2A Rana 37 GILSLVKGVAKLAGKGLAKEGGKFGLELIACKIAKQC esculenta 494 Esculentin-2B Rana 37 GLFSILRGAAKFASKGLGKDLTKLGVDLVACKISKQC berlandieri 495 Esculentin-2B Rana 37 GIFSLVKGAAKLAGKGLAKEGGKFGLELIACKIAKQC esculenta 496 Esculentin-2L Rana 37 GILSLFTGGIKALGKTLFKMAGKAGAEHLACKATNQC luteiventris 497 Esculentin-2P Rana 37 GFSSIFRGVAKFASKGLGKDLARLGVNLVACKISKQC pipiens 498 Formaecin 1 Myrmecia 16 GRPNPVNNKPTPHPRL gulosa 499 Formaecin 2 Myrmecia 16 GRPNPVNTKPTPYPRL gulosa 500 Gaegurin-1 Rana 33 SLFSLIKAGAKFLGKNLLKQGACYAACKASKQC rugosa 501 Gaegurin-2 Rana 33 GIMSIVKDVAKNAAKEAAKGALSTLSCKLAKTC rugosa 502 Gaegurin-3 Rana 33 GIMSIVKDVAKTAAKEAAKGALSTLSCKLAKTC rugosa 503 Gaegurin-4 Rana 80 MFTMKKSLLFLFFLGTISLSLCEEERSADEDDGGEM precursor rugosa TEEEVKRGILDTLKQFAKGVGKDLVKGAAQGVLSTV SCKLAKTC 504 Gaegurin-5 Rana 65 MFTLKKSLLLLFFLGTISLSLCEEERNADEEEKRDVE precursor rugosa VEKRFLGALFKVASKVLPSVFCAITKKC 505 Gaegurin-6 Rana 24 FLPLLAGLAANFLPTIICKISYKC rugosa 506 Gal-1 alpha Gallus 65 MRIVYLLLPFILLLAQGAAGSSQALGRKSDCFRKNG gallus FCAFLKCPYLTLISGKCSRFHLCCKRIWG 507 gallinacin Gallus 39 GRKSDCFRKSGFCAFLKCPSLTLISGKCSRFYLCCK gallus RIW 508 gallinacin Gallus 36 LFCKGGSCHFGGCPSHLIKVGSCFGFRSCCKWPW gallus NA 509 Gallinacin 1 Gallus 39 GRKSDCFRKNGFCAFLKCPYLTLISGKCSRFHLCCK alpha gallus RIW 510 Gallinacin 1 Gallus 65 MRIVYLLLPFILLLAQGAAGSSQALGRKSDCFRKSG precursor gallus FCAFLKCPSLTLISGKCSRFYLCCKRIWG 511 Gallinacin 2 Gallus 64 MRILYLLFSLLFLALQVSPGLSSPRRDMLFCKGGSC precursor gallus HFGGCPSHLIKVGSCFGFRSCCKWPWNA 512 Gastric Sus scrofa 42 YAEGTFISDYSIAMDKIRQQDFVNWLLAQKGKKSD inhibitory WKHNITQ polypeptide (GIP) (Glucose- dependent insulinotropic polypeptide) 513 Gloverin Hyalophora 130 DVTWDKNIGNGKVFGTLGQNDDGLFGKAGFKQQF cecropia FNDDRGKFEGQAYGTRVLGPAGGTTNFGGRLDWS DKNANAALDISKQIGGRPNLSASGAGVWDFDKNTR LSAGGSLSTMGRGKPDVGVHAQFQHDF 514 Gomesin Acanthoscurria 18 QCRRLCYKQRCVTYCRGR gomesiana 515 GP- Cavia 31 RRCICTTRTCRFPYRRLGTCLFQNRVYTFCC CS2 =CORTICO STATIC peptide (Fragment) 516 Hadrurin Hadrurus 41 GILDTIKSIASKVWNSKTVQDLKRKGINWVANKLGVS aztecus PQAA 517 Hemiptericin Pyrrhocoris 133 DVELKGKGGENEGFVGLKAQRNLYEDDRTSLSGTV apterus KGQSQWKDPYPAQHAGMARLDGTRTLIENDRTKV TGSGFAQREVATGMRPHDSFGVGVEATHNIYKGKN GEVDVFGGVQRQWNTPDRHQARGGIRWRF 518 Hepcidin Mus 83 MALSTRTQAACLLLLLLASLSSTTYLQQQMRQTTEL antimicrobial musculus QPLHGEESRADIAIPMQKRRKRDINFPICRFCCQCC peptide 2 NKPSCGICCEE 519 hepcidin Danio rerio 91 MKLSNVFLAAVVILTCVCVFQITAVPFIQQVQDEHHV antimicrobial ESEELQENQHLTEAEHRLTDPLVLFRTKRQSHLSLC peptide RFCCKCCRNKGCGYCCKF precursor 520 Hepcidin Morone 85 MKTFSVAVAVAVVLAFICLQESSAVPVTEVQELEEP precursor chrysops × MSNEYQEMPVESWKMPYNNRHKRHSSPGGCRFC Morone CNCCPNMSGCGVCCRF saxatilis 521 Hepcidin Mus 83 MALSTRTQAACLLLLLLASLSSTTYLHQQMRQTTEL precursor musculus QPLHGEESRADIAIPMQKRRKRDTNFPICIFCCKCC NNSQCGICCKT 522 Hepcidin Rattus 84 MALSTRIQAACLLLLLLASLSSGAYLRQQTRQTTALQ precursor norvegicus PWHGAESKTDDSALLMLKRRKRDTNFPICLFCCKC CKNSSCGLCCIT 523 Hepcidin Oncorhynchus 61 LQVLTEEVGSIDSPVGEHQQPGGESMRLPEHFRFK precursor mykiss RXSHLSLCRWCCNCCHNKGXGFCCKF (Fragment) 524 Histone H2A Bufo 39 AGRGKQGGKVRAKAKTRSSRAGLQFPVGRVHRLL [Contains: gargarizans RKGNY Buforin I; Buforin II] (Fragment) 525 Histone H2A Hippoglossus 51 SGRGKTGGKARAKAKTRSSRAGLQFPVGRVHRLL [Contains: hippoglossus RKGNYAHRVGAGAPVYL Hipposin] (Fragment) 526 Histone H2B-1 Ictalurus 20 PDPAKTAPKKGSKKAVTKXA (Antibacterial punctatus histone-like protein 1) (HLP- 1) (Fragment) 527 Histone H2B-3 Ictalurus 17 PDPAKTAPKKKSKKAVT (Antibacterial punctatus histone-like protein 3) (HLP- 3) (Fragment) 528 holotricin 1 Holotrichia 43 VTCDLLSLQIKGIAINDSACAAHCLAMRRKGGSCKQ diomphalia GVCVCRN 529 Holotricin 2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFDEADIE precursor diomphalia PQLSPAELHHGSIRERRSLQPGAPSFPMPGSQLPT SVSGNVEKQGRNTIATIDAQHKTDRYDVRGTWTKV VDGPGRSKPNFRIGGSYRW 530 holotricin 2 Holotrichia 127 MMKLVIALCLIGISAAYVVPVYYEIYPEDATFDEADIE precursor diomphalia PQLSPAELHHGSIRERRSLQPGAPSLSQLPTSVSGN VEKQGRPMPGNTIATIDAQHKTDRYDVRGTVDGPG RSKPNFRIGGSWTKVYRW 531 Holotricin 3 Holotrichia 104 MNKLIILGLACIIAVASAMPYGPGDGHGGGHGGGHG precursor diomphalia GGHGNGQGGGHGHGPGGGFGGGHGGGHGGGG RGGGGSGGGGSPGHGAGGGYPGGHGGGHHGGY QTHGY 532 Hymenoptaecin Apis 129 MKFIVLVLFCAVAYVSAQAELEPEDTMDYIPTRFRR precursor mellifera QERGSIVIQGTKEGKSRPSLDIDYKQRVYDKNGMT GDAYGGLNIRPGQPSRQHAGFEFGKEYKNGFIKGQ SEVQRGPGGRLSPYFGINGGFRF 533 Indolicidin Bos taurus 14 ILPWKWPWWPWRRX 534 Indolicidin Bos taurus 144 MQTQRASLSLGRWSLWLLLLGLVVPSASAQALSYR precursor EAVLRAVDQLNELSSEANLYRLLELDPPPKDNEDLG TRKPVSFTVKETVCPRTIQQPAEQCDFKEKGRVKQ CVGTVTLDPSNDQFDLNCNELQSVILPWKWPWWP WRRG 535 Insect Defensin Protophormia 40 ATCDLLSGTGINHSACAAHCLLRGNRGGYCNGKGV A (NMR, 10 terraenovae CVCRN Structures) - Chai 536 Interferon- Mus sp. 15 SETAPAETPAPAKAE activated antimicrobial protein (Fragment) 537 Japonicin-1 Rana 14 FFPIGVFCKIFKTC japonica 538 Japonicin-2 Rana 21 FGLPMLSILPKALCILLKRKC japonica 539 Lactoferricin Bos taurus 25 FKCRRWQWRMKKLGAPSITCVRRAF 540 lactoferrin Sus scrofa 703 MKLFIPALLFLGTLGLCLAAPKKGVRWCVISTAEYSK precursor CRQWQSKIRRTNPMFCIRRASPTDCIRAIAAKRADA VTLDGGLVFEADQYKLRPVAAEIYGTEENPQTYYYA VAVVKKGFNFQNQLQGRKSCHTGLGRSAGWNIPIG LLRRFLDWAGPPEPLQKAVAKFFSQSCVPCADGNA YPNLCQLCIGKGKDKCACSSQEPYFGYSGAFNCLH KGIGDVAFVKESTVFENLPQKADRDKYELLCPDNTR KPVEAFRECHLARVPSHAVVARSVNGKENSIWELL YQSQKKFGKSNPQEFQLFGSPGQQKDLLFRDATIG FLKIPSKIDSKLYLGLPYLTAIQGLRETAAEVEARQAK VVWCAVGPEELRKCRQWSSQSSQNLNCSLASTTE DCIVQVLKGEADAMSLDGGFIYTAGKCGLVPVLAEN QKSRQSSSSDCVHRPTQGYFAVAVVRKANGGITW NSVRGTKSCHTAVDRTAGWNIPMGLLVNQTGSCKF DEFFSQSCAPGSQPGSNLCALCVGNDQGVDKCVP NSNERYYGYTGAFRCLAENAGDVAFVKDVTVLDNT NGQNTEEWARELRSDDFELLCLDGTRKPVTEAQNC HLAVAPSHAVVSRKEKAAQVEQVLLTEQAQFGRYG KDCPDKFCLFRSETKNLLFNDNTECLAQLQGKTTYE KYLGSEYVTAIANLKQCSVSPLLEACAFMMR 541 Lactotransferrin Bos taurus 708 MKLFVPALLSLGALGLCLAAPRKNVRWCTISQPEWF precursor KCRRWQWRMKKLGAPSITCVRRAFALECIRAIAEKK (Lactoferrin) ADAVTLDGGMVFEAGRDPYKLRPVAAEIYGTKESP [Contains: QTHYYAVAVVKKGSNFQLDQLQGRKSCHTGLGRS Lactoferricin B AGWIIPMGILRPYLSWTESLEPLQGAVAKFFSASCV (LFCIN B)] PCIDRQAYPNLCQLCKGEGENQCACSSREPYFGYS GAFKCLQDGAGDVAFVKETTVFENLPEKADRDQYE LLCLNNSRAPVDAFKECHLAQVPSHAVVARSVDGK EDLIWKLLSKAQEKFGKNKSRSFQLFGSPPGQRDLL FKDSALGFLRIPSKVDSALYLGSRYLTTLKNLRETAE EVKARYTRVVWCAVGPEEQKKCQQWSQQSGQNV TCATASTTDDCIVLVLKGEADALNLDGGYIYTAGKC GLVPVLAENRKSSKHSSLDCVLRPTEGYLAVAVVKK ANEGLTWNSLKDKKSCHTAVDRTAGWNIPMGLIVN QTGSCAFDEFFSQSCAPGADPKSRLCALCAGDDQ GLDKCVPNSKEKYYGYTGAFRCLAEDVGDVAFVKN DTVWENTNGESTADWAKNLNREDFRLLCLDGTRK PVTEAQSCHLAVAPNHAVVSRSDRAAHVKQVLLHQ QALFGKNGKNCPDKFCLFKSETKNLLFNDNTECLAK LGGRPTYEEYLGTEYVTAIANLKKCSTSPLLEACAFL TR 542 Lebocin ½ Bombyx 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPPTQRPI precursor mori IRTARQAGQEPLWLYQGDNVPRAPSTADHPILPSKI DDVQLDPNRRYVRSVTNPENNEASIEHSHHTVDTG LDQPIESHRNTRDLRFLYPRGKLPVPTPPPFNPKPIY IDMGNRYRRHASDDQEELRQYNEHFLIPRDIFQE 543 Lebocin 3 Bombyx 179 MYKFLVFSSVLVLFFAQASCQRFIQPTFRPPPTQRPI precursor (LEB mori TRTVRQAGQEPLWLYQGDNVPRAPSTADHPILPSKI 3) DDVQLDPNRRYVRSVTNPENNEASIEHSHHTVDIGL DQPIESHRNTRDLRFLYPRGKLPVPTLPPFNPKPIYI DMGNRYRRHASEDQEELRQYNEHFLIPRDIFQE 544 lectin-L6 Limulus 221 VQWHQIPGKLMHITATPHFLWGVNSNQQIYLCRQP polyphemus CYDGQWTQISGSLKQVDADDHEVWGVNRNDDIYK RPVDGSGSWVRVSGKLKHVSASGYGYIWGVNSND QIYKCPKPCNGAWTQVNGRLKQIDGGQSMVYGVN SANAIYRRPVDGSGSWQQISGSLKHITGSGLSEVFG VNSNDQIYRCTKPCSGQWSLIDGRLKQCDATGNTIV GVNSVDNIYRSG 545 Limulus factor D Tachypleus 394 MKVLLLVAFLLGTTLAYPQDDDGPVWGGSSNDNDD tridentatus GGISSRVGNPQSGFGNCECVPYYLCKDNNIIIDGSG LLDPRKKPVASKEPKLSARLGPEGPSGCGPFHVCCI APETSTVKPYTHQCGFRNVNGINKRILSPNGKDLSE FGEWPWQGAVLKVEGKVNIFQCGAVLIDSYHLLTV AHCVYKFTLENAFPLKVRLGEWDTQNTNEFLKHED YEVEKIYIHPKYDDERKNLWDDIAILKLKAEVSFGPHI DTICLPNNQEHFAGVQCVVTGWGKNAYKNGSYSN VLREVHVPVITNDRCQELLRKTRLSEWYVLYENFIC AGGESNADSCKGDGGGPLTCWRKDGTYGLAGLVS WGINCGSPNVPGVYVRVSNYLDWITKITGRPISDYW PRS 546 Lingual Bos taurus 64 MRLHHLLLALLFLVLSAGSGFTQGVRNSQSCRRNK antimicrobial GICVPIRCPGSMRQIGTCLGAQVKCCRRK peptide precursor 547 Liver-expressed Bos taurus 77 MWHLKLFAVLMICLLLLAQVDGSPIPQQSSAKRRPR antimicrobial RMTPFWRAVSLRPIGASCRDDSECITRLCRKRRCS peptide 2 LSVAQE precursor (LEAP-2) 548 Liver-expressed Macaca 77 MWHLKLCAVLMIFLLLLGQTDGSPIPEVSSAKRRPR antimicrobial mulatta RMTPFWRGVSLRPIGASCRDDSECITRLCRKRRCS peptide 2 LSVAQE precursor (LEAP-2) 549 Liver-expressed Mus 76 MLQLKLFAVLLTCLLLLGQVNSSPVPEVSSAKRSRR antimicrobial musculus MTPFWRGVSLRPIGASCRDDSECITRLCRKRRCSL peptide 2 SVAQE precursor (LEAP-2) 550 Liver-expressed Sus scrofa 77 MWHLKLFAVLVICLLLAVQVHGSPIPELSSAKRRPR antimicrobial RMTPFWRAVSLRPIGASCRDDSECLTRLCRKRRCS peptide 2 LSVAQE precursor (LEAP-2) 551 Liver-expressed Cavia 71 SVVLLICLLLLGQVDGSPVPEKSSVKKRLRRMTPFW antimicrobial porcellus RGVSLRPIGASCRDDSECITRLCKKRRCSLSVAQE peptide 2 precursor (LEAP-2) (Fragment) 552 Liver-expressed Sus scrofa 77 MWHLKLFAVLVICLLLAVQVHGSPIPELSSAKRRPR antimicrobial RITPFWRAVSLRPIGASCRDDSECLTRLCRKRRCSL protein 2 SVAQE 553 Lysozyme Heliothis 141 MQKLTLFVVALAAVVLHCEAKQFSRCGLVQELRRQ virescens GFPEDKLGDWVCLVENESARKTDKVGTVNKNGSR DYGLYQINDKYWCSNTSTPGKDCNVTCAEMLLDDI TKASTCAKKIYKRHKFEAWYGWKNHCKGKTLPDIS NC 554 lysozyme (EC Alopochen 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKY 3.2.1.17) aegyptiacus ESGFNTQATNRNTDGSTDYGILQINSRWWCNDGKT PRAKNVCGIPCSVLLRSDITEAVKCAKRIVSDGNGM NAWVAWRNRCKGTDVSQWIRGCRL 555 lysozyme (EC Chrysolophus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKF 3.2.1.17) pictus ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRT PGSRNLCHIPCSALLSSDITASVNCAKKIVSDGNGM NAWVAWRNRCKGTDVNAWTRGCRL 556 lysozyme (EC Lophophorus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKF 3.2.1.17) impejanus ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRT PGSRNLCNIPCSALLSSDITASVNCAKKIVSDGNGM NAWVAWRNRCKGTDVHAWIRGCRL 557 lysozyme (EC Manduca 120 KHFSRCELVHELRRQGFPENLMRDWVCLVENESS 3.2.1.17) sexta RYTDKVGRVNKNGSRDYGLFQINDKYWCSNGSTP GKDCNVKCSDLLIDDITKASTCAKKIYKRHKFQAWY GWRNHCQGSLPDISSC 558 lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCLTKWE 3.2.1.17) 1 SSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKT PNAVDGCHVSCSELMENNIAKAVACAKHIVSEQGIT AWVAWKSHCRDHDVSSYVEGCSL 559 lysozyme (EC Rattus 148 MKALLVLGFLLLSASVQAKIYERCEFARTLKRNGMS 3.2.1.17) 1 norvegicus GYYGVSLADWVCLAQHESNYNTQARNYNPGDQST precursor DYGIFQINSRYWCNDGKTPRAKNACGIPCSALLQDD ITQAIQCAKRVVRDPQGIRAWVAWQRHCKNRDLSG YIRNCGV 560 lysozyme (EC Bos taurus 129 KTFKRCELARTLKNLGLAGYKGVSLANWMCLAKGE 3.2.1.17) 14d, SNYNTQAKNYNPGSKSTDYGIFQINSKWWCNDGKT tracheal PKAVNGCGVSCSALLKDDITQAVACAKKIVSQQGIT AWVAWKNKCRNRDLTSYVKGCGV 561 lysozyme (EC Cervus axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCLTKWE 3.2.1.17) 2 SSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKT PNAVDGCHVACSELMENDIAKAVACAKQIVREQGIT AWVAWKSHCRDHDVSSYVEGCTL 562 lysozyme (EC Ovis aries 129 KVFERCELARTLKELGLDGYKGVSLANWLCLTKWE 3.2.1.17) 2 SSYNTKATNYNPGSESTDYGIFQINSKWWCNDGKT PNAVDGCHVSCSALMENDIEKAVACAKHIVSEQGIT AWVAWKSHCRDHDVSSYVEGCTL 563 lysozyme (EC Ovis aries 129 KVFERCELARTLKKLGLDDYKGVSLANWLCLTKWE 3.2.1.17) 3 SGYNTKATNYNPGSESTDYGIFQINSKWWCNDGKT PNAVDGCHVSCSALMENDIEKAVACAKHIVSEQGIT AWVAWKSHCRDHDVSSYVEGCTL 564 lysozyme (EC Bos taurus 130 KVFERCELARSLKRFGMDNFRGISLANWMCLARWE 3.2.1.17) 5a, SNYNTQATNYNAGDQSTDYGIFQINSHWWCNDGK tracheal TPGAVNACHLPCGALLQDDITQAVACAKRVVSDPQ GIRAWVAWRSHCQNQDLTSYIQGCGV 565 lysozyme (EC Drosophila 140 MKAFIVLVALASGAPALGRTMDRCSLAREMSNLGV 3.2.1.17) B melanogaster PRDQLARWACIAEHESSYRTGVVGPENYNGSNDY precursor GIFQINDYYWCAPPSGRFSYNECGLSCNALLTDDIT HSVRCAQKVLSQQGWSAWSTWHYCSGWLPSIDD CF 566 lysozyme (EC Papio sp. 130 KIFERCELARTLKRLGLDGYRGISLANWVCLAKWES 3.2.1.17) c DYNTQATNYNPGDQSTDYGIFQINSHYWCNDGKTP GAVNACHISCNALLQDNITDAVACAKRVVSDPQGIR AWVAWRNHCQNRDVSQYVQGCGV 567 lysozyme (EC Numida 129 KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKF 3.2.1.17) c meleagris ESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGR [validated] TPGSRNLCNIPCSALQSSDITATANCAKKIVSDGDG MNAWVAWRKHCKGTDVRVWIKGCRL 568 lysozyme (EC Coturnix 129 KVYGRCELAAAMKRHGLDKYQGYSLGNWVCAAKF 3.2.1.17) C japonica ESNFNTQATNRNTDGSTDYGILQINSRWWCNDGRT precursor PGSRNLCNIPCSALLSSDITASVNCAKKIVSDVHGM NAWVAWRNRCKGTDVNVWIRGCRL 569 lysozyme (EC Hyalophora 132 CRSWQFALHCDAKRFTRCGLVQELRRRGFDETLM 3.2.1.17) c cecropia SNWVCLVENESGRFTDKIGKVNKNGSRDYGLFQIN precursor DKYWCSKGSTPGKDCNVTCNQLLTDDISVAATCAK KIYKRHKFDAWYGWKNHCQHGLPDISDC 570 lysozyme (EC Phasianus 147 MRSLLILVLCFLPLAAPGKVYGRCELAAAMKRMGLD 3.2.1.17) c colchicus NYRGYSLGNWVCAAKFESNFNTGATNRNTDGSTD precursor YGILQINSRWWCNDGRTPGSKNLCHIPCSALLSSDI [validated] TASVNCAKKIVSDGDGMNAWVAWRKHCKGTDVNV WIRGCRL 571 lysozyme (EC Drosophila 140 MKAFIVLVALALAAPALGRTLDRCSLAREMSNLGVP 3.2.1.17) E melanogaster RDQLARWACIAEHESSYRTGVVGPENYNGSNDYGI precursor FQINDYYWCAPPSGRFSYNECGLSCNALLTDDITHS VRCAQKVLSQQGWSAWSTWHYCSGWLPSIDDCF 572 lysozyme (EC Rhea 185 RTNCYGDVSRIDTTGASCKTAKPEKLNYCGVAASR 3.2.1.17) g americana KIAERDLRSMDRYKTLIKKVGQKLCVEPAVIAGIISRE SHAGKALKNGWGDNGNGFGLMQVDRRSHKPVGE WNGERHLIQGTEILISMIKAMQRKFPRWTKEQQLKG GISAYNAGPGNVRTYERMDIGTTHDDYANDVVARA QYYKQHGY 573 lysozyme (EC Casuarius 185 QTGCYGVVNRIDTTGASCETAKPEKLNYCGVAASR 3.2.1.17) g casuarius KIAEGDLQSMDRYKTLIKKVGQKLCVDPAVIAGIISR [validated] ESHAGKALKDGWGDNGNGFGLMQVDKRSHTPVG KWNGERHLTQGTEILISMIKKIQKKFPRWTKEQQLK GGISAYNAGSGNVRTYERMDIGTTHNDYANDVVAR AQYYKQHGY 574 lysozyme (EC Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMSNLGV 3.2.1.17) melanogaster PRDQLNKWACIAEHESSYRTGVVGPENYNGSNDY precursor GIFQINDYYWCAPPSGRFSYNECGLSCNALLTDDIT HSVRCAQKVLSQQGWSAWSTWHYCSGWLPSIDD CF 575 lysozyme (EC Opisthocomus 145 MLFFGFLLAFLSAVPGTEGEIISRCELVKILREHGFE 3.2.1.17) hoazin GFEGTTIADWICLVQHESDYNTEAYNNNGPSRDYGI precursor, FQINSKYWCNDGKTSGAVDGCHISCSELMTNDLED stomach DIKCAKKIARDAHGLTPWYGWKNHCEGRDLSSYVK GC 576 lysozyme (EC Drosophila 139 MKAFFALVLLPLPLCLAGRTLDRCSLAREMADLGVP 3.2.1.17) S melanogaster RDQLDKWTCIAQHESDYRTWVVGPANSDGSNDYG precursor IFQINDLYWCQADGRFSYNECGLSCNALLTDDITNS VRCAQKVLSQQGWSAWAVWHYCSGWLPSIDECF 577 lysozyme (EC Drosophila 81 PNTDGSNDYGIFQINDLYWCQPSSGKFSHNGCDVS 3.2.1.17) X melanogaster CNALLTDDIKSSVRCALKVLGQQGWSAWSTWHYC SGYLPPIDDCFV 578 Lysozyme Drosophila 140 MKAFIVLVALACAAPAFGRTMDRCSLAREMSNLGV A/C/D precursor melanogaster PRDQLARWACIAEHESSYRTGVVGPENYNGSNDY (EC 3.2.1.17) GIFQINDYYWCAPPSGRFSYNECGLSCNALLTDDIT (1,4-beta-N- HSVRCAQKVLSQQGWSAWSTWHYCSGWLPSIDD acetylmuramidase CF A/C) 579 Lysozyme C Callipepla 129 KVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAKF (EC 3.2.1.17) californica ESNFNSQATNRNTDGSTDYGVLQINSRWWCNDGR (1,4-beta-N- TPGSRNLCNIPCSALLSSDITATVNCAKKIVSDGNG acetylmuramidase MNAWVAWRNRCKGTDVHAWIRGCRL C) 580 Lysozyme C Colinus 130 MKVFGRCELAAAMKRHGLDNYRGYSLGNWVCAAK (EC 3.2.1.17) virginianus FESNFNSQATNRNTDGSTDYGVLQINSRWWCNDG (1,4-beta-N- KTPGSRNLCNIPCSALLSSDITATVNCAKKIVSDGNG acetylmuramidase MNAWVAWRNRCKGTDVQAWIRGCRL C) 581 Lysozyme C Columba 127 KDIPRCELVKILRRHGFEGFVGKTVANWVCLVKHES (EC 3.2.1.17) livia GYRTTAFNNNGPNSRDYGIFQINSKYWCNDGKTRG (1,4-beta-N- SKNACNINCSKLRDDNIADDIQCAKKIAREARGLTP acetylmuramidase WVAWKKYCQGKDLSSYVRGC C) 582 Lysozyme C Equus 129 KVFSKCELAHKLKAQEMDGFGGYSLANWVCMAEY (EC 3.2.1.17) asinus ESNFNTRAFNGKNANGSYDYGLFQLNSKWWCKDN (1,4-beta-N- KRSSSNACNIMCSKLLDDNIDDDISCAKRVVRDPKG acetylmuramidase MSAWKAWVKHCKDKDLSEYLASCNL C) 583 Lysozyme C Ortalis 129 KIYKRCELAAAMKRYGLDNYRGYSLGNWVCAARYE (EC 3.2.1.17) vetula SNYNTQATNRNSNGSTDYGILQINSRWWCNDGRT (1,4-beta-N- PGTKNLCHISCSALMGADIAPSVRCAKRIVSDGDGM acetylmuramidase NAWVAWRKHCKGTDVSTWIKDCKL C) 584 Lysozyme C Oryctolagus 130 KIYERCELARTLKKLGLDGYKGVSLANWMCLAKWE (EC 3.2.1.17) cuniculus SSYNTRATNYNPGDKSTDYGIFQINSRYWCNDGKT (1,4-beta-N- PRAVNACHIPCSDLLKDDITQAVACAKRVVSDPQGI acetylmuramidase RAWVAWRNHCQNQDLTPYIRGCGV C) 585 Lysozyme C Syrmaticus 129 KVYGRCELAAAMKRLGLDNFRGYSLGNWVCAAKF (EC 3.2.1.17) soemmerringii ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRT (1,4-beta-N- PGSRNLCNIPCSALLSSDTIASVNCAKKIVSDGNGM acetylmuramidase NAWVAWRKRCKGTDVNAWTRGCRL C) (CPL) 586 Lysozyme C Felis catus 20 KIFTKCELARKLRAEGMDGF (EC 3.2.1.17) (1,4-beta-N- acetylmuramidase C) (Fragment) 587 Lysozyme C Pseudocheirus 49 SKMKKCEFAKIAKEQHMDGYHGVSLADWVCLVNN (EC 3.2.1.17) peregrinus ESDFNTKAINRNKGI (1,4-beta-N- acetylmuramidase C) (Fragment) 588 Lysozyme C Lophura 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKY (EC 3.2.1.17) leucomelanos ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGKT (1,4-beta-N- PGSRNLCHIPCSALLSSDITASVNCAKKIVSDGNGM acetylmuramidase) NAWVAWRNRCKGTDVSVWTRGCRL 589 Lysozyme C Pavo 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKF (EC 3.2.1.17) cristatus ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRT (1,4-beta-N- PGSRNLCNIPCSALLSSDITASVNCAKKIVSDRNGM acetylmuramidase) NAWVAWRNRCKGTDVHAWIRGCRL 590 Lysozyme C Phasianus 130 GKVYGRCELAAAMKRMGLDNYRGYSLGNWVCAAK (EC 3.2.1.17) versicolor FESNFNTGATNRNTDGSTDYGILQINSRWWCNDGR (1,4-beta-N- TPGSKNLCHIPCSALLSSDITASVNCAKKIVSDGDG acetylmuramidase) MNAWVAWRKHCKGTDVNVWIRGCRL 591 Lysozyme C Syrmaticus 129 KVYGRCELAAAMKRLGLDNYRGYSLGNWVCAAKF (EC 3.2.1.17) reevesi ESNFNTHATNRNTDGSTDYGILQINSRWWCNDGRT (1,4-beta-N- PGSRNLCHISCSALLSSDITASVNCAKKIVSDRNGM acetylmuramidase) NAWVAWRNRCKGTDVNAWIRGCRL 592 Lysozyme C 1 Cervus axis 129 KVFERCELARTLKELGLDGYKGVSLANWLCLTKWE and 2 (EC SSYNTKATNYNPGSESTDYGIFQINSKWWCDDGKT 3.2.1.17) (1,4- PNAVDGCHVACSELMENNIDKAVTCAKQIVREQGIT beta-N- AWVAWKSHCRGHDVSSYVEGCTL acetylmuramidase C) 593 Lysozyme C 1 Bos taurus 147 MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDG precursor (EC YKGVSLANWLCLTKWESSYNTKATNYNPGSESTDY 3.2.1.17) (1,4- GIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDI beta-N- AKAVACAKQIVSEQGITAWVAWKSHCRDHDVSSYV acetylmuramidase EGCTL C) 594 Lysozyme C 2 Bos taurus 147 MKALVILGFLFLSVAVQGKVFERCELARTLKKLGLD precursor (EC GYKGVSLANWLCLTKWESSYNTKATNYNPSSESTD 3.2.1.17) (1,4- YGIFQINSKWWCNDGKTPNAVDGCHVSCSELMEN beta-N- DIAKAVACAKHIVSEQGITAWVAWKSHCRDHDVSS acetylmuramidase YVEGCTL C) 595 Lysozyme C 3 Bos taurus 147 MKALIILGFLFLSVAVQGKVFERCELARTLKKLGLDG precursor (EC YKGVSLANWLCLTKWESSYNTKATNYNPSSESTDY 3.2.1.17) (1,4- GIFQINSKWWCNDGKTPNAVDGCHVSCSELMENDI beta-N- AKAVACAKHIVSEQGITAWVAWKSHCRDHDVSSYV acetylmuramidase QGCTL C) 596 Lysozyme C I Tachyglossus 125 KILKKQELCKNLVAQGMNGYQHITLPNWVCTAFHES (EC 3.2.1.17) aculeatus SYNTRATNHNTDGSTDYGILQINSRYWCHDGKTPG (1,4-beta-N- SKNACNISCSKLLDDDITDDLKCAKKIAGEAKGLTPW acetylmuramidase VAWKSKCRGHDLSKFKC C) 597 Lysozyme C II Oncorhynchus 144 MRAVVVLLLVAVASAKVYDRCELARALKASGMDGY precursor (EC mykiss AGNSLPNWVCLSKWESSYNTQATNRNTDGSTDYGI 3.2.1.17) (1,4- FQINSRYWCDDGRTPGAKNVCGIRCSQLLTADLTV beta-N- AIRCAKRVVLDPNGIGAWVAWRLHCQNQDLRSYVA acetylmuramidase GCGV C) 598 Lysozyme C Coturnix 147 MRSLLVLVLCFLPLAALGKVYGRCELAAAMKRHGLD precursor (EC japonica KYQGYSLGNWVCAAKFESNFNTQATNRNTDGSTD 3.2.1.17) (1,4- YGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDI beta-N- TASVNCAKKIVSDVHGMNAWVAWRNRCKGTDVNA acetylmuramidase WIRGCRL C) 599 Lysozyme C Meleagris 147 MRSLLILVLCFLPLAALGKVYGRCELAAAMKRLGLD precursor (EC gallopavo NYRGYSLGNWVCAAKFESNFNTHATNRNTDGSTD 3.2.1.17) (1,4- YGILQINSRWWCNDGRTPGSKNLCNIPCSALLSSDI beta-N- TASVNCAKKIASGGNGMNAWVAWRNRCKGTDVHA acetylmuramidase WIRGCRL C) 600 Lysozyme C Presbytis 148 MKALTILGLVLLSVTVQGKIFERCELARTLKKLGLDG precursor (EC entellus YKGVSLANWVCLAKWESGYNTEATNYNPGDESTD 3.2.1.17) (1,4- YGIFQINSRYWCNNGKTPGAVDACHISCSALLQNNI beta-N- ADAVACAKRVVSDPQGIRAWVAWRNHCQNKDVSQ acetylmuramidase YVKGCGV C) 601 Lysozyme C Gallus 147 MRSLLILVLCFLPLAALGKVFGRCELAAAMKRHGLD precursor (EC gallus NYRGYSLGNWVCAAKFESNFNTQATNRNTDGSTD 3.2.1.17) (1,4- YGILQINSRWWCNDGRTPGSRNLCNIPCSALLSSDI beta-N- TASVNCAKKIVSDGNGMNAWVAWRNRCKGTDVQA acetylmuramidase WIRGCRL C) (Allergen Gal d 4) (Gal d IV) 602 Lysozyme C, Rattus 148 MKALLVLGFLLLSASVQAKVFKHCELARILRSSALAG type 2 norvegicus YRGVSLENWMCMAQHESNFDTEAINYNSTDQSTD precursor (EC YGIFQINSRYWCNDGKTPRAVNACGIPCSALLQDDI 3.2.1.17) (1,4- TQAIQCAKRVVRDPQGIRAWVAWQRHCQNRDLSG beta-N- YIRNCGV acetylmuramidase C) 603 Lysozyme C, Mus 148 MKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMA type M musculus GYYGVSLADWVCLAQHESNYNTRATNYNRGDQST precursor (EC DYGIFQINSRYWCNDGKTPRAVNACGINCSALLQD 3.2.1.17) (1,4- DITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLS beta-N- QYIRNCGV acetylmuramidase C) 604 Lysozyme C, Mus 148 MKALLTLGLLLLSVTAQAKVYNRCELARILKRNGMD type P musculus GYRGVKLADWVCLAQHESNYNTRATNYNRGDRST precursor (EC DYGIFQINSRYWCNDGKTPRSKNACGINCSALLQD 3.2.1.17) (1,4- DITAAIQCAKRVVRDPQGIRAWVAWRTQCQNRDLS beta-N- QYIRNCGV acetylmuramidase C) 605 Lysozyme C-1 Anas 147 MKALLTLVFCLLPLAAQGKVYSRCELAAAMKRLGLD precursor (EC platyrhynchos NYRGYSLGNWVCAANYESGFNTQATNRNTDGSTD 3.2.1.17) (1,4- YGILQINSRWWCDNGKTPRSKNACGIPCSVLLRSDI beta-N- TEAVRCAKRIVSDGDGMNAWVAWRNRCRGTDVSK acetylmuramidase WIRGCRL C) 606 Lysozyme C-3 Anas 129 KVYERCELAAAMKRLGLDNYRGYSLGNWVCAANY (EC 3.2.1.17) platyrhynchos ESSFNTQATNRNTDGSTDYGILEINSRWWCDNGKT (1,4-beta-N- PRAKNACGIPCSVLLRSDITEAVKCAKRIVSDGDGM acetylmuramidase) NAWVAWRNRCKGTDVSRWIRGCRL 607 Lysozyme G Anser 185 RTDCYGNVNRIDTTGASCKTAKPEGLSYCGVSASK (EC 3.2.1.17) anser KIAERDLQAMDRYKTIIKKVGEKLCVEPAVIAGIISRE (1,4-beta-N- SHAGKVLKNGWGDRGNGFGLMQVDKRSHKPQGT acetylmuramidase) WNGEVHITQGTTILINFIKTIQKKFPSWTKDQQLKGG (Goose-type ISAYNAGAGNVRSYARMDIGTTHDDYANDVVARAQ lysozyme) YYKQHGY 608 Lysozyme G Cygnus 185 RTDCYGNVNRIDTTGASCKTAKPEGLSYCGVPASK (EC 3.2.1.17) atratus TIAERDLKAMDRYKTIIKKVGEKLCVEPAVIAGIISRE (1,4-beta-N- SHAGKVLKNGWGDRGNGFGLMQVDKRSHKPQGT acetylmuramidase) WNGEVHITQGTTILTDFIKRIQKKFPSWTKDQQLKG (Goose-type GISAYNAGAGNVRSYARMDIGTTHDDYANDVVARA lysozyme) QYYKQHGY 609 Lysozyme G Struthio 185 RTGCYGDVNRVDTTGASCKSAKPEKLNYCGVAAS (EC 3.2.1.17) camelus RKIAERDLQSMDRYKALIKKVGQKLCVDPAVIAGIIS (1,4-beta-N- RESHAGKALRNGWGDNGNGFGLMQVDRRSHKPV acetylmuramidase) GEWNGERHLMQGTEILISMIKAIQKKFPRWTKEQQL (Goose-type KGGISAYNAGPGNVRSYERMDIGTTHDDYANDVVA lysozyme) RAQYYKQHGY 610 Lysozyme G Gallus 211 MLGKNDPMCLVLVLLGLTALLGICQGGTGCYGSVS precursor (EC gallus RIDTTGASCRTAKPEGLSYCGVRASRTIAERDLGSM 3.2.1.17) (1,4- NKYKVLIKRVGEALCIEPAVIAGIISRESHAGKILKNG beta-N- WGDRGNGFGLMQVDKRYHKIEGTWNGEAHIRQGT acetylmuramidase) RILIDMVKKIQRKFPRWTRDQQLKGGISAYNAGVGN (Goose-type VRSYERMDIGTLHDDYSNDVVARAQYFKQHGY lysozyme) 611 Lysozyme P Drosophila 141 MKAFLVICALTLTAVATQARTMDRCSLAREMSKLGV precursor (EC melanogaster PRDQLAKWTCIAQHESSFRTGVVGPANSNGSNDY 3.2.1.17) (1,4- GIFQINNKYWCKPADGRFSYNECGLSCNALLTDDIT beta-N- NSVKCARKIQRQQGWTAWSTWKYCSGSLPSINSCF acetylmuramidase P) 612 Lysozyme Chlamys 137 MMYFVLLCLLATGTTYGAHNFATGIVPQSCLECICK precursor islandica TESGCRAIGCKFDVYSDSCGYFQLKQAYWEDCGR PGGSLTSCADDIHCSSQCVQHYMSRYIGHTSCSRT CESYARLHNGGPHGCEHGSTLGYWGHVQGHGC 613 Lysozyme Bombyx 137 MQKLIIFALVVLCVGSEAKTFTRCGLVHELRKHGFEE precursor (EC mori NLMRNWVCLVEHESSRDTSKTNTNRNGSKDYGLF 3.2.1.17) (1,4- QINDRYWCSKGASPGKDCNVKCSDLLTDDITKAAK beta-N- CAKKIYKRHRFDAWYGWKNHCQGSLPDISSC acetylmuramidase) 614 Lysozyme Hyalophora 139 MTKYVILLAVLAFALHCDAKRFTRCGLVQELRRLGF precursor (EC cecropia DETLMSNWVCLVENESGRFTDKIGKVNKNGSRDYG 3.2.1.17) (1,4- LFQINDKYWCSKGTTPGKDCNVTCNQLLTDDISVAA beta-N- TCAKKIYKRHKFDAWYGWKNHCQHGLPDISDC acetylmuramidase) 615 Maculatin 1.1 Litoria 21 GLFGVLAKVAAHVVPAIAEHF [Contains: genimaculata Maculatin 1.1.1] 616 Maculatin 1.2 Litoria 23 GLFGVLAKVASHVVPAIAEHFQA genimaculata 617 Maculatin 2.1 Litoria 18 GFVDFLKKVAGTIANVVT genimaculata 618 Maculatin 3.1 Litoria 26 GLLQTIKEKLESLESLAKGIVSGIQA genimaculata 619 Magainins Xenopus 303 MFKGLFICSLIAVICANALPQPEASADEDMDEREVR precursor laevis GIGKFLHSAGKFGKAFVGEIMKSKRDAEAVGPEAFA DEDLDEREVRGIGKFLHSAKKFGKAFVGEIMNSKRD AEAVGPEAFADEDLDEREVRGIGKFLHSAKKFGKAF VGEIMNSKRDAEAVGPEAFADEDLDEREVRGIGKFL HSAKKFGKAFVGEIMNSKRDAEAVGPEAFADEDFD EREVRGIGKFLHSAKKFGKAFVGEIMNSKRDAEAVG PEAFADEDLDEREVRGIGKFLHSAKKFGKAFVGEIM NSKRDAEAVDDRRWVE 620 Melittin-like Rana 22 FIGSALKVLAGVLPSIVSWVKQ peptide (MLP) temporaria 621 Metchnikowin Drosophila 52 MQLNLGAIFLALLGVMATTTSVLAEPHRRQGPIFDT melanogaster RPSPFNPNQPRPGPIY 622 Metchnikowin Drosophila 52 MQLNLGAIFLALLGVMATATSVLAEPHRHQGPIFDT precursor melanogaster RPSPFNPNQPRPGPIY 623 MGD1 Mytilus 57 CPNNYQCHRHCKSIPGRCGGYCGGWHRLRCTCYR antimicrobial galloprovin CGGRREDVEDIFDIFDNEAADRF peptide cialis (Fragment) 624 Misgurin Misgurnus 21 RQRVEELSKFSKKGAAARRRK anguillicau datus 625 Moricin 1 Bombyx 66 MNILKFFFVFIVAMSLVSCSTAAPAKIPIKAIKTVGKA precursor mori VGKGLRAINIASTANDVFNFLKPKKRKH 626 Moricin 2 Bombyx 66 MNILKLFFVFIVAMSLVSCSTAAPAKIPIKAIKTVGKAV precursor mori GKGLRAINIASTANDVFNFLKPKKRKH 627 myeloid Ovis aries 160 METQRASLSLGRRSLWLLLLGLVLASARAQALSYRE antimicrobial AVLRAVDQLNEKSSEANLYRLLELDPPPKQDDENS peptide 29 NIPKPVSFRVKETVCPRTSQQPAEQCDFKENGLLKE precursor CVGTVTLDQVGNNFDITCAEPQSVRGLRRLGRKIAH GVKKYGPTVLRIIRIAG 628 Myeloid Ovis aries 165 METQRAGLSLGRWSLRLLLLGLVLPSASTRSFSYRE antimicrobial AVLRAVDQFNERSAEANLYRLLELDPPPEQDAEDR peptide GARKPVSFKVKETVCPRTSQQPVEQCDFRKNGLVK precursor QCVGTVTRYWIRGDFDITCKDIQNVGLFGRLRDSLQ RGGQKILEKAERIGDRIKDIFRG 629 Myticin A Mytilus 96 MKATILLAVLVAVFVAGTEAHSHACTSYWCGKFCGT precursor galloprovincialis ASCTHYLCRVLHPGKMCACVHCSRVNNPFRVNQV AKSINDLDYTPIMKSMENLDNGMDML 630 Myticin B Mytilus 96 MKATMLLAVVVAVFVAGTEAHPHVCTSYYCSKFCG precursor galloprovincialis TAGCTRYGCRNLHRGKLCFCLHCSRVKFPFGATQD AKSMNELEYTPIMKSMENLDNGMDML 631 Mytilin A Mytilus 34 GCASRCKAKCAGRRCKGWASASFRGRCYCKCFRC edulis 632 Mytilin B Mytilus 34 SCASRCKGHCRARRCGYYVSVLYRGRCYCKCLRC edulis 633 Mytilin B Mytilus 103 MKAAVILAIALVAILAVHEAEASCASRCKGHCRARRC antimicrobial galloprovincialis GYYVSVLYRGRCYCKCLRCSSEHSMKFPENEGSS peptide PSDMMPQMNENENTEFGQDMPTGETEQGETGI precursor 634 Mytimycin Mytilus 33 DCCRKPFRKHCWDCTAGTPYYGYSTRNIFGCTC (Fragment) edulis 635 Neutrophil Rattus 94 MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQEQLV antibiotic norvegicus MEDQDISISFGGDKGTALQDADVKAGVTCYCRRTR peptide NP-1 CGFRERLSGACGYRGRIYRLCCR precursor (Neutrophil defensin 1) (RatNP-1) 636 Neutrophil Rattus 94 MRTLTLLTALLLLALHTQAKSPQGTAEEAPDQEQLV antibiotic norvegicus MEDQDISISFGGDKGTALQDADVKAGVTCYCRSTR peptide NP-2 CGFRERLSGACGYRGRIYRLCCR precursor (Neutrophil defensin 2) (RatNP-2) 637 Neutrophil Rattus 87 MRTLTLLTTLLLLALHTQAESPQGSTKEAPDEEQDIS antibiotic norvegicus VFFGGDKGTALQDAAVKAGVTCSCRTSSCRFGERL peptide NP-3 SGACRLNGRIYRLCC precursor (Neutrophil defensin 3) (RatNP-3a) 638 Neutrophil Rattus 87 MRTLILLTTLLLLALHTQAESPQGSTKEAPDEEQDIS antibiotic norvegicus VFFGGDKGTALQDAAVKAGVTCSCRTSSCRFGERL peptide NP-3 SGACRLNGRIYRLCC precursor (Neutrophil defensin 3) (RatNP-3b) 639 Neutrophil Oryctolagus 95 MRTLALLAAILLVTLQAQAELHSGMADDGVDQQQP antibiotic cuniculus RAQDLDVAVYIKQDETSPLEVLGAKAGVSCTCRRFS peptide NP-4 CGFGERASGSCTVNGVRHTLCCRR precursor (Microbicidal peptide NP-4) 640 Neutrophil Rattus 93 MRTLTLLITLLLLALHTQAESPQERAKAAPDQDMVM antibiotic norvegicus EDQDIFISFGGYKGTVLQDAVVKAGQACYCRIGACV peptide NP-4 SGERLTGACGLNGRIYRLCCR precursor (Neutrophil defensin 4) (RatNP-4) 641 Neutrophil Oryctolagus 95 MRTLALLAAILLVTLQAQAELHSGMADDGVDQQQP antibiotic cuniculus RAQDLDVAVYIKQDETSPLEVLGAKAGVFCTCRGFL peptide NP-5 CGSGERASGSCTINGVRHTLCCRR precursor (Microbicidal peptide NP-5) 642 neutrophil beta- Bos taurus 60 MRLHHLLLALLFLVLSAASGISGPLSCGRNGGVCIPI defensin 12 RCPVPMRQIGTCFGRPVKCCRSW 643 neutrophil beta- Bos taurus 54 MRLHHLLLVLLFLVLSAGSGFTQVVRNPQSCRWNM defensin 5 GVCIPISCPGNMRQIGTCS 644 Neutrophil Cavia 178 MGTPRDAASGGPRLLLPLLLLLLLTPATAWVLSYQQ cationic porcellus AVQRAVDGINKNLADNENLFRLLSLDTQPPGDNDP antibacterial YSPKPVSFTIKETVCTKMLQRPLEQCDFKENGLVQR polypeptide of CTGTVTLDSAFNVSSLSCLGGRRFRRMVGLRKKFR 11 kDa KTRKRIQKLGRKIGKTGRKVWKAWREYGQIPYPCRI 645 Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDTKMKG cationic peptide porcellus DREDHVAVISFWEEESTSLEDAGAGAGRRCICTTRT 1 precursor CRFPYRRLGTCIFQNRVYTFCC (Neutrophil defensin) (GPNP) (Corticostatic peptide GP- CS1) (CP-1) 646 Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDTKMKG cationic peptide porcellus DREDHVAVISFWEEESTSLQDAGAGAGRRCICTTR 1B precursor TCRFPYRRLGTCIFQNRVYTFCC (Neutrophil defensin) (CP- 1B) (GNCP) 647 Neutrophil Cavia 93 MRTVPLFAACLLLTLMAQAEPLPRAADHSDTKMKG cationic peptide porcellus DREDHVAVISFWEEESTSLQDAGAGAGRRCICTTR 2 precursor TCRFPYRRLGTCLFQNRVYTFCC (CP-2) (GNCP) (GNCP-2) 648 Neutrophil Mesocricetus 33 VTCFCRRRGCASRERHIGYCRFGNTIYRLCCRR defensin 1 auratus (HANP-1) 649 Neutrophil Mesocricetus 31 CFCKRPVCDSGETQIGYCRLGNTFYRLCCRQ defensin 2 auratus (HANP-2) 650 Neutrophil Macaca 30 ACYCRIPACLAGERRYGTCFYMGRVWAFCC defensin 2 mulatta (RMAD-2) 651 Neutrophil Mesocricetus 33 VTCFCRRRGCASRERLIGYCRFGNTIYGLCCRR defensin 3 auratus (HANP-3) 652 Neutrophil Mesocricetus 33 VTCFCKRPVCDSGETQIGYCRLGNTFYRLCCRQ defensin 4 auratus (HANP-4) 653 Neutrophil Macaca 96 MRTLVILAAILLVALQAQAEPLQARTDEATAAQEQIP defensins 1, 3 mulatta TDNPEVVVSLAWDESLAPKDSVPGLRKNMACYCRI and 8 precursor PACLAGERRYGTCFYLGRVWAFCC (RMAD) 654 Neutrophil Macaca 94 MRTIAILAAILLFALLAQAKSLQETADDMTQEQPGE defensins 4 and mulatta DDQDLAVSFEENGLSTLRASGSQARRTCRCRFGR 5 precursor CFRRESYSGSCNINGRIFSLCCR (RMAD) 655 Neutrophil Macaca 94 MRTIAILAAILLFALLAQAKSLQETADEMTQEQPGE defensins 6 and mulatta DDQDLAVSFEENGLSTLRASGSQARRTCRCRFGR 7 precursor CFRRESYSGSCNINGRISSLCCR 656 NK-lysin Sus scrofa 129 PGLAFSGLTPEHSALARAHPCDGEQFCQNLAPEDP precursor (NKL) QGDQLLQREELGLICESCRKIIQKLEDMVGPQPNED (Fragment) TVTQAASRVCDKMKILRGVCKKIMRTFLRRISKDILT GKKPQAICVDIKICKEKTGLI 657 Nonhistone Oncorhynchus 69 PKRKSATKGDEPARRSARLSARPVPKPAAKPKKAA chromosomal mykiss APKKAVKGKKAAENGDAKAEAKVQAAGDGAGNAK protein H6 (Histone T) [Contains: Oncorhyncin III] 658 Oligosaccharide- Bos taurus 190 MSRRYTPLAWVLLALLGLGAAQDCGSIVSRGKWGA binding protein LASKCSQRLRQPVRYVVVSHTAGSVCNTPASCQR QAQNVQYYHVRERGWCDVGYNFLIGEDGLVYEGR GWNTLGAHSGPWNPIAIGISFMGNYMHRVPPASA LRAAQSLLACGAARGYLTPNYEVKGHRDVQQTLSP GDELYKIIQQWPHYRRV 659 Opistoporin 1 Opistophthalmus 44 GKVWDWIKSTAKKLWNSEPVKELKNTALNMKNLV carinatus AEKIGATPS 660 Opistoporin 2 Opistophthalmus 44 GKVWDWIKSTAKKLWNSEPVKELKNTALNAAKNFV carinatus AEKIGATPS 661 Pandinin 1 Pandinus 44 GKVWDWIKSAAKKIWSSEPVSQLKGQVLNAAKNYV imperator AEKIGATPT 662 Pandinin 2 Pandinus 24 FWGALAKGALKLIPSLFSSFSKKD imperator 663 Parabutoporin Parabuthus 45 FKLGSFLKKAWKSKLAKKLRAKGKEMLKDYAKGLLE schlechteri GGSEEVPGQ 664 Penaeidin-1 Litopenaeus 50 YRGGYTGPIPRPPPIGRPPLRLVVCACYRLSVSDAR (Pen-1) (P1) vannamei NCCIKFGSCCHLVK 665 Penaeidin-2a Litopenaeus 72 MRLVVCLVFLASFALVCQGEAYRGGYTGPIPRPPPI precursor (Pen- vannamei GRPPFRPVCNACYRLSVSDARNCCIKFGSCCHLVKG 2a) (Pen-2) (P2) 666 Penaeidin-2b Litopenaeus 72 MRLVVCLVFLASFALVCQGEAYRGGYTGPIPRPPPI precursor (Pen- vannamei GRPPLRPVCNACYRLSVSDARNCCIKFGSCCHLVKG 2b) 667 Penaeidin-2d Litopenaeus 72 MRLVVCLVFLASFALVCQGGAQRGGFTGPIPRPPP precursor (Pen- setiferus HGRPPLGPICNACYRLSFSDVRICCNFLGKCCHLVKG 2d) 668 Penaeidin-3a Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLG 3a) (P3-a) RCCHVGKGYSG 669 Penaeidin-3b Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPVPRPPP precursor (Pen- vannamei FVRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRL 3b) (P3-b) GRCCHVGKGYSG 670 Penaeidin-3c Litopenaeus 81 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPFV precursor (Pen- vannamei RPVPGGPIGPYNGCPVSCRGISFSQARSCCSRLGR 3c) (P3-c) CCHVGKGYSG 671 Penaeidin-3d Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPISCRGISFSQARSCCSRLGR 3d) CCHVGKGYSG 672 Penaeidin-3e Litopenaeus 82 MRLVVCLVFLAPFALVCHGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLG 3e) RCCHVGKGYSG 673 Penaeidin-3f Litopenaeus 82 MRLVACLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPISCRGISFSQARSCCSRLGR 3f) CCHVGKGYSG 674 Penaeidin-3g Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPISPYNGCPVSCRGISFSQARSCCSRLG 3g) RCCHVGKGYSG 675 Penaeidin-3h Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPISCRGISFSQARSYCSRLGR 3h) CCHVGKGYSG 676 Penaeidin-3i Litopenaeus 82 MRLVVCLVFLASFALVCQGQVYKGGYTRPIPRPPPF precursor (Pen- vannamei VRPLPGGPIGPYNGRPVSCRGISFSQARSCCSRLG 3i) RCCHVGKGYSG 677 Penaeidin-3j Litopenaeus 81 MRLVVCLVFLASFALVCQGQVYKGGYTRPVPRPPF precursor (Pen- vannamei VRPLPGGPIGPYNGCPVSCRGISFSQARSCCSRLG 3j) RCCHVGKGYSG 678 Penaeidin-3k Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPILRPYVR precursor (Pen- setiferus PVVSYNACTLSCRGITTTQARSCCTRLGRCCHVAK 3k) GYSG 679 Penaeidin-3l Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPILRPYVR precursor (Pen- setiferus PVVSYNVCTLSCRGITTTQARSCCTRLGRCCHVAK 3l) GYSG 680 Penaeidin-3m Litopenaeus 75 MRLVVCLVFLASFALVCQGQGCKGPYTRPILRPYVR precursor (Pen- setiferus PVVSYNACTLSCRGITTTQARSCCTRLGRCCHVAK 3m) GYSG 681 Penaeidin-3n Litopenaeus 75 MRLVVCLVFLASFALVCQGQGYKGPYTRPILRPYVR precursor (Pen- setiferus PVVSYNACTLSCRGITTTQARSCSTRLGRCCHVAK 3n) GYSG 682 Penaeidin-4a Litopenaeus 67 MRLVVCLVFLASFALVCQGHSSGYTRPLPKPSRPIFI precursor (Pen- vannamei RPIGCDVCYGIPSSTARLCCFRYGDCCHRG 4a) 683 Penaeidin-4c Litopenaeus 67 MRLVVCLVFLASFALVCQGYSSGYTRPLPKPSRPIFI precursor (Pen- vannamei RPIGCDVCYGIPSSTARLCCFRYGDCCHRG 4c) 684 Penaeidin-4d Litopenaeus 67 MRLLVCLVFLASFAMVCQGHSSGYTRPLRKPSRPIF precursor (Pen- setiferus IRPIGCDVCYGIPSSTARLCCFRYGDCCHLG 4d) 685 Phormicin Protophormia 94 MKFFMVFVVTFCLAVCFVSQSLAIPADAANDAHFVD precursor terraenovae GVQALKEIEPELHGRYKRATCDLLSGTGINHSACAA (Insect HCLLRGNRGGYCNGKGVCVCRN defensins A and B) 686 Phylloxin Phyllomedusa 64 MVFLKKSLLLVLFVGLVSLSICEENKREEHEEIEENK precursor bicolor EKAEEKRGWMSKIASGIGTFLSGMQQG 687 Pleurocidin Pseudople 25 GWGSFFKKAAHVGKHVGKAALHTYL uronectes americanus 688 Pleurocidin 2 Pseudople 68 MKFTATFLMMAIFVLMVEPGECGWGSFFKKAAHVG precursor uronectes KHVGKAALTHYLGDKQELNKRAVDEDPNVIVFE americanus 689 Pleurocidin Pseudople 68 MKFTATFLMIAIFVLMVEPGECGWGSFFKKAAHVGK prepropolypeptide uronectes HVGKAALTHYLGDKQELNKRAVDEDPNVIVFE americanus 690 Pleurocidin Pseudople 68 MKFTATFLMMFIFVLMVEPGECGWGSIFKHGRHAA prepropolypeptide uronectes KHIGHAAVNHYLGEQQDLDKRAVDEDPNVIVFE americanus 691 Pleurocidin Pseudople 60 MKFTATFLMIAIFVLMVEPGECGWGSFFKKAAHVGK prepropolypeptide uronectes HVGKAALTHYLGDKQELNKRAVDE (Fragment) americanus 692 Pleurocidin Pseudople 60 MKFTATFLMMFIFVLMVEPGECGWGSIFKHGRHAA prepropolypeptide uronectes KHIGHAAVNHYLGEQQDLDKRAVDE (Fragment) americanus 693 Pleurocidin-like Pseudople 89 MKFTATFLLLFIFVLMVDLGEGRRKKKGSKRKGSKG prepropolypeptide uronectes KGSKGKGRWLERIGKAGGIIIGGALDHLGQGQVQG (Fragment) americanus PDYDYQEGEELNKRAVDE 694 Pleurocidin-like Pseudople 72 MKFTATFLLLFIFVLMVDLGEGRRKRKWLRRIGKGV prepropolypeptide uronectes KIIGGAALDHLGQGQVQGQDYDYQEGQELNKRAVDE (Fragment) americanus 695 Pleurocidin-like Pseudople 61 MKFTATFLVLSLVVLMAEPGECFLGALIKGAIHGGRF prepropolypeptide uronectes IHGMIQNHHGYDEQQELNKRAVDE (Fragment) americanus 696 Polyphemusin I Limulus 18 RRWCFRVCYRGFCYRKCR polyphemus 697 Polyphemusin II Limulus 18 RRWCFRVCYKGFCYRKCR polyphemus 698 Ponericin G1 Pachycondyla 30 GWKDWAKKAGGWLKKKGPGMAKAALKAAMQ goeldii 699 Ponericin G2 Pachycondyla 30 GWKDWLKKGKEWLKAKGPGIVKAALQAATQ goeldii 700 Ponericin G3 Pachycondyla 30 GWKDWLNKGKEWLKKKGPGIMKAALKAATQ goeldii 701 Ponericin G4 Pachycondyla 29 DFKDWMKTAGEWLKKKGPGILKAAMAAAT goeldii 702 Ponericin G5 Pachycondyla 30 GLKDWVKIAGGWLKKKGPGILKAAMAAATQ goeldii 703 Ponericin G6 Pachycondyla 18 GLVDVLGKVGGLIKKLLP goeldii 704 Ponericin G7 Pachycondyla 19 GLVDVLGKVGGLIKKLLPG goeldii 705 Ponericin L1 Pachycondyla 24 LLKELWTKMKGAGKAVLGKIKGLL goeldii 706 Ponericin L2 Pachycondyla 24 LLKELWTKIKGAGKAVLGKIKGLL goeldii 707 Ponericin W1 Pachycondyla 25 WLGSALKIGAKLLPSVVGLFKKKKQ goeldii 708 Ponericin W2 Pachycondyla 25 WLGSALKIGAKLLPSVVGLFQKKKK goeldii 709 Ponericin W3 Pachycondyla 26 GIWGTLAKIGIKAVPRVISMLKKKKQ goeldii 710 Ponericin W4 Pachycondyla 26 GIWGTALKWGVKLLPKLVGMAQTKKQ goeldii 711 Ponericin W5 Pachycondyla 24 FWGALIKGAAKLIPSVVGLFKKKQ goeldii 712 Ponericin W6 Pachycondyla 20 FIGTALGIASAIPAIVKLFK goeldii 713 Preprodefensin Boophilus 74 MRGIYICLXFVLXCGLVSGLADVPAESEMAHLRVRR microplus GFGCPFNQGACHRHCRSIRRRGGYCAGLIKQTCTC YRN 714 preprodefensin Ixodes 76 MKVLAVSLAFLLIAGLISTSLAQNEEGGEKELVRVRR ricinus GGYYCPFFQDKCHRHCRSFGRKAGYCGGFLKKTCI CVMK 715 Probable Riptortus 678 MRSPRVIHLACVIAYIVAVEAGDKPVYLPRPTPPRPI antibacterial clavatus HPRLAREVGWELEGQGLSPLSEAELLPEVRERRSP peptide VDKGGYLPRPTPPRPVYRSRRDASLESELSPLSVA polyprotein EVLPEVRERRSPVDKGGYLPRPTPPRPVYRSRRDA precursor SLESELSPLSEAEVLPEVRERRSPVDKGGYLPRPTP PRPVYRSRRVASLESELSPLSEAEVLPEVRERRSPV DKGGYLPRPTPPRPVYRSRRDASLESELSPLSEEE VLPEVRERGSPVDKGGYLPRPTPPRPVYRSRRDAS LESELSPLSVAEDLPEVRERRSPVDKGGYLPRPTPP RPVYRSRRDASLESELSPLSEAEVLPEVRERRSPV DKGGYLPRPTPPRPVYRSRRDASLESELSPLSEAE VLPEVRERRSPVDKGGYLPRPTPPRPVYRSRRDAS LESELSPLSEAEVLPEVRERRSPVDKGGYLPRPTPP RPVYRSRRDASLESELSPLSEAEVLPEVRERRSPV DKGGYLPRPTPPRPVYRSRRDATLESELSPSSEAE VLPEVRERRSPVDKGGYLPRPTPPRPVYRSRRDAS LESELSPLSEAEVLPEVRERRSPVDKGGYLPRPTPP RPVYRSRRDASLESELSPLSEAEGLPEVRERRSPG GQGGYLPRPTPRTPLCRSRRDANLDAEQSPVSEG VVLPEVR 716 Probable Riptortus 150 MHIARFCLLSSMAVLALSAGYVSGAVIEIPDEILDSA antibacterial clavatus RFISLYSDGLRQKRQLNLSGPGSEHAGTIRLDGQRN peptide IFDNGRTRVDGTGSYQLDYARGMKPIHGAGLGAEV precursor NHNIWRGRGGQSLDLYGGATRQFNFGNRPNEWG AHGGIRYNF 717 Proenkephalin Bos taurus 263 MARFLGLCTWLLALGPGLLATVRAECSQDCATCSY A precursor RLARPTDLNPLACTLECEGKLPSLKTWETCKELLQL [Contains: TKLELPPDATSALSKQEESHLLAKKYGGFMKRYGG Synenkephalin; FMKKMDELYPLEVEEEANGGEVLGKRYGGFMKKD Met-enkephalin AEEDDGLGNSSNLLKELLGAGDQREGSLHQEGSDA (Opioid growth EDVSKRYGGFMRGLKRSPHLEDETKELQKRYGGF factor) (OGF); MRRVGRPEWWMDYQKRYGGFLKRFAEPLPSEEE Met-enkephalin- GESYSKEVPEMEKRYGGFMRF Arg-Gly-Leu; Leu- enkephalin; Enkelytin; Met- enkephalin-Arg- Phe] 718 Prophenin-1 Sus scrofa 212 LLLLALVVPSASAQALSYREAVLRAVDRLNEQSSEA precursor (PF- NLYRLLELDQPPKADEDPGTPKPVSFTVKETVCPRP 1) (C6) TRQPPELCDFKENGRVKQCVGTVTLDQIKDPLDITC (Fragment) NEGVRRFPWWWPFLRRPRLRRQAFPPPNVPGPRF PPPNFPGPRFPPPNFPGPRFPPPNFPGPRFPPPNF PGPPFPPPIFPGPWFPPPPPFRPPPFGPPRFPGRR 719 Prophenin-2 Sus scrofa 228 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR precursor (PF- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 2) (PR-2) (C12) GTPKPVSFTVKETVCPRPTRRPPELCDFKENGRVK (Prophenin-1 QCVGTVTLDQIKDPLDITCNEGVRRFPWWWPFLRR like) PRLRRQAFPPPNVPGPRFPPPNVPGPRFPPPNFPG PRFPPPNFPGPRFPPPNFPGPPFPPPIFPGPWFPP PPPFRPPPFGPPRFPGRR 720 Protegrin 1 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR precursor (PG- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 1) (Neutrophil GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK peptide 1) QCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRR RFCVCVGRG 721 Protegrin 2 Sus scrofa 147 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR precursor (PG- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 2) GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRR RFCICVG 722 Protegrin 3 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR precursor (PG- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 3) GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLDQIKDPLDITCNEVQGVRGGGLCYCRR RFCVCVGRG 723 Protegrin 4 Sus scrofa 149 METQRASLCLGRWSLWLLLLALVVPSASAQALSYR precursor (PG- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 4) GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRG WICFCVGRG 724 Protegrin 5 Sus scrofa 149 METQRASLCLGRWSLWLLLLGLVVPSASAQALSYR precursor (PG- EAVLRAVDRLNEQSSEANLYRLLELDQPPKADEDP 5) GTPKPVSFTVKETVCPRPTRQPPELCDFKENGRVK QCVGTVTLDQIKDPLDITCNEVQGVRGGRLCYCRP RFCVCVGRG 725 Protegrin-1 Sus scrofa 19 RGGRLCYCRRRFCVCVGRX 726 Pseudin 1 Pseudis 24 GLNTLKKVFQGLHEAIKLINNHVQ paradoxa 727 Pseudin 2 Pseudis 24 GLNALKKVFQGIHEAIKLINNHVQ paradoxa 728 Pseudin 3 Pseudis 23 GINTLKKVIQGLHEVIKLVSNHE paradoxa 729 Pseudin 4 Pseudis 23 GINTLKKVIQGLHEVIKLVSNHA paradoxa 730 Putative Litopenaeus 188 MKGIKAVILCGLFTAVLAGKYRGFGQPLGGLGVPGG antimicrobial setiferus GVGVGVGGGLGGGLGGGLGGGLGGGLGGGLGGL peptide GGGLGGLGGGLGGGLGGGLGGGLGGGLGGSHGT SDCRYWCKTPEGQAYCCESAHEPETPVGTKPLDC PQVRPTCPRFHGPPTTCSNDYKCAGLDKCCFDRCL GEHVCKPPSFFGQQIFG 731 Putative Litopenaeus 123 MKGLGVILCCVLAVVPAHAGPGGFPGGVPGRFPSA antimicrobial setiferus TAPPATCRRWCKTPENQAYCCETIFEPEAPVGTKP peptide LDCPQVRPTCPRFHGPPVTCSSDYKCGGVDKCCF DRCLGEHVCKPPSFYSQFP 732 Putative Litopenaeus 141 MKGLGVILCCVLAVVPAHAGPGGFSGGVPGGFPG antimicrobial setiferus GRPGGFPGGVPGGFPSATAPPATCRRWCKTPENQ peptide AYCCETIFEPEAPVGTKPLDCPQVRPTCPPTRFGG RPVTCSSDYKCGGLDKCCFDRCLGEHVCKPPSFYS QFR 733 Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGLGGPG antimicrobial vannamei GGVGVGGGFPGGGLGVGGGLGVGGGLGVGGGLG peptide VGGGLGTGTSDCRYWCKTPEGQAYCCESAHEPET PVGTKILDCPQVRPTCPRFHGPPTTCSNDYKCAGL DKCCFDRCLGEHVCKPPSFFGSQVFG 734 Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGLGGPG antimicrobial vannamei GGVGVGGGFPGGGLGVGGGLGVGGGLGVGGGLG peptide VGGGLGTGTSDCRYWCKTPEGQAYCCESAHEPET PVGTKPLDCPQVRPTCPRFHGPPTTCSNDYKCAGL DKCCFDRCLGEHVCKPPSFFGSQVFG 735 Putative Litopenaeus 169 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGLGGPG antimicrobial vannamei GGVGVGGGFPGGGLGVGGGLGVGGGLGVGGGLG peptide VGGGLGVGGGLGTGTSDCRYWCKTPEGQAYCCE SAHEPETPVGTKILDCPQVRPTCPRFHGPPTTCSN DYKCAGLDKCCFDRCLGEHVCKPPSFFGSQVFG 736 Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGQPFGGLGGPG antimicrobial vannamei GSVGVGGGFPGGGLGVGGGLGVGGGLGVGGGLG peptide VGGGLGTGTSDCRYWCKTPEGQAYCCESAHEPET PVGTKPLDCPQVRPTCPRFHGPPTTCSNDYKCAGL DKCCFDRCLGEHVCKPPSFFGSQVFG 737 Putative Litopenaeus 151 MKGIKAVILCGLFTAVLAGKFRGFGRPFGGLGGPG antimicrobial vannamei GGVGVGGGFPGGGLGVGGGLGVGGGLGTGTSDC peptide RYWCKTPEGQAYCCESAHEPETPVGTKPLDCPQV RPTCPRFHGPPTTCSNDYKCAGLDKCCFDRCLGEH VCKPPSFFGSQVFG 738 Putative Litopenaeus 163 MKGIKAVILCGLFTAVLAGKFRGFGRPFGGLGGPG antimicrobial vannamei GGVGVGGGFPGGGLGVGGGLGVGGGLGVGGGLG peptide VGGGLGTGTSDYRYWCKTPEGQAYCCESAHEPET PVGTKPLDCPQVRPTCPRFHGPPTTCSNDYKCAGL DKCCFDRCLGEHVCKPPSFFGSQVFG 739 Putative beta Mus 79 MKTFLFLFAVLFFLDPAKNAFFDEKCSRVNGRCTAS defensin musculus CLKNEELVALCQKNLKCCVTVQPCGKSKSNQSDEG SGHMGTWG 740 Putative beta Mus 63 MPQTFFVFCFLFFVFLQLFPGTGEIAVCETCRLGRG defensin musculus KCRRACIESEKIVGWCKLNFFCCRERI 741 Putative beta Mus 64 MRIFSLIVAGLVLLIQLYPAWGTLYRRFLCKKMNGQ defensin musculus CEAECFTFEQKIGTCQANFLCCRKRKEH 742 Putative beta Mus 67 MRTLCSLLLICCLLFSYTTPAANSIIGVSEMERCHKK defensin musculus GGYCYFYCFSSHKKIGSCFPEWPRCCKNIK 743 Putative beta Mus 77 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQLARC defensin musculus YKFGGFCYNSMCPPHTKFIGNCHPDHLHCCINMKE LEGST 744 Putative beta Mus 73 MRTLCSLLLICCLLFSYTTPAVGDLKHLILKAQLTRCY defensin musculus KFGGFCHYNICPGNSRFMSNCHPENLRCCKNIKQF 745 Putative Mesobuthus 61 MTYAILIIVSLLLISDRISNVVDKYCSENPLDCNEHCL potassium martensii KTKNQIGICHGANGNEKCSCMES channel blocker TXKs2 746 PYLa/PGLa Xenopus 64 MYKQIFLCLIIAALCATIMAEASAFADADEDDDKRYV precursor laevis RGMASKAGAIAGKIAKVALKALGRRDS 747 Pyrrhocoricin Pyrrhocoris 20 VDKGSYLPRPTPPRPIYNRN apterus 748 Ranalexin Rana 66 MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDNPD precursor catesbeiana ERDVEVEKRFLGGLIKIVPAMICAVTKKC 749 Ranalexin-1CA Rana 20 FLGGLMKAFPALICAVTKKC clamitans 750 Ranalexin-1CB Rana 20 FLGGLMKAFPAIICAVTKKC clamitans 751 Ranatuerin-1C Rana 25 SMLSVLKNLGKVGLGLVACKINKQC clamitans 752 RANATUERIN- Rana 28 GLLDTIKGVAKTVAASMLDKLKCKISGC 2B berlandieri 753 Ranatuerin-2CA Rana 31 GLFLDTLKGAAKDVAGKLLEGLKCKIAGCKP clamitans 754 Ranatuerin-2CB Rana 27 GLFLDTLKGLAGKLLQGLKCIKAGCKP clamitans 755 RANATUERIN- Rana 32 GILSSIKGVAKGVAKNVAAQLLDTLKCKITGC 2LB luteiventris 756 RANATUERIN- Rana 27 LMDTVKNVAKNLAGHMLDKLKCKITGC 2P pipiens 757 RANATUREIN- Rana 32 GILDSFKGVAKGVAKDLAGKLLDKLKCKITGC 2LA luteiventris 758 Rhinocerosin Oryctes 142 MMKLYIVFGFIAFSAAYVVPEGYYEPEYYPADGYES precursor rhinoceros ERVARASPAELIFDEDLADEPEVEEPQYYIRTRRSL QPGAPNFPMPGSQLPTSITSNIEKQGPNTAATINAQ HKTDRYDVGATWSKVIRGPGRSKPNWSIGGTYRW 759 Royalisin Apis 95 MKIYFIVGLLFMAMVAIMAAPVEDEFEPLEHFENEER precursor mellifera ADRHRRVTCDLLSFKGQVNDSACAANCLSLGKAGG (Defensin) HCEKVGCICRKTSFKDLWDKRFG 760 Rugosin A Rana 33 GLLNTFKDWAISIAKGAGKGVLTTLSCKLDKSC rugosa 761 Rugosin B Rana 33 SLFSLIKAGAKFLGKNLLKQGAQYAACKVSKEC rugosa 762 Rugosin C Rana 37 GILDSFKQFAKGVGKDLIKGAAQGVLSTMSCKLAKTC rugosa 763 Sapecin B Sarcophaga 88 MKFLTSLLLLFVVVMVSAVNLSMAKESANQLTERLQ precursor peregrina ELDGAAIQEPAELNRHKRLTCEIDRSLCLLHCRLKG YLRAYCSQQKVCRCVQ 764 Sapecin C Sarcophaga 40 ATCDLLSGIGVQHSACALHCVFRGNRGGYCTGKGI peregrina CVCRN 765 Sapecin Sarcophaga 94 MKSFIVLAVTLCLAAFFMGQSVASPAAAAEESKFVD precursor peregrina GLHALKTIEPELHGRYKRATCDLLSGTGINHSACAA HCLLRGNRGGYCNGKAVCVCRN 766 Sarcotoxin IA Sarcophaga 63 MNFQNIFIFVALILAVFAGQSQAGWLKKIGKKIERVG precursor peregrina QHTRDATIQGLGIAQQAANVAATARG 767 Sarcotoxin IB Sarcophaga 63 MNFNKVFIFVALILAVFAGQSQAGWLKKIGKKIERVG precursor peregrina QHTRDATIQVIGVAQQAANVAATARG 768 Sarcotoxin IC Sarcophaga 39 GWLRKIGKKIERVGQHTRDATIQVLGIAQQAANVAA peregrina TAR 769 Sarcotoxin ID Sarcophaga 40 GWIRDFGKRIERVGQHTRDATIQTIAVAQQAANVAA peregrina TLKG 770 Sarcotoxin II-1 Sarcophaga 26 MKSFVLFAACMAIIALGSLAHAYPQKLPVPIPPPSNP precursor peregrina PVAVLQNSVATNSKGGQDVSVKLSATNLGNNHVQP IAEVFAEGNTKGGNVLRGATVGVQGHGLGASVTKT QTDTKIKGLDFQPQLSSSTLALQGDRLGASISRDVN RGVSDTFTKSVSANVFRNDNHNLDATVFRSDVRQN NGFNFQKTGGMLDYSHANGHGLNAGLTHFSGIGN QANVGGSSTLFKSNDGSLSLKANAGGSQWLSGPF SNQRDYNVGLSLTHHGCGG 771 Sarcotoxin II-2 Sarcophaga 294 MKSFVFFAACFAIVALNSLAHAYPQKLPVPIPPPTNP precursor peregrina PVAAFHNSVATNSKGGQDVSVKLAATNLGNKHVQP IAEVFAKGNTQGGNVLRGATVGVQGHGLGASVTKT QDGIAESFRKQAEANLRLGDSASLIGKVSQTDTKIK GIDFKPQLSSSSLALQGDRLGASISRDVNRGVSDTL TKSISANVFRNDNHNLDASVFRSDVRQNNGFNFQK TGGMLDYSHANGHGLNAGLTRFSGIGNQANVGGY STLFRSNDGLTSLKANAGGSQWLSGPFANQRDYSF GLGLSHNAWRG 772 Sarcotoxin II-3 Sarcophaga 294 MKSFVLFAACMAIVALSSLAHAYPQKLPVPIPPPTNP precursor peregrina PVAAFHNSVATNSKGGQDVSVKLAATNLGNKHVQP IAEVFAEGNTKGGNVIRGATVGVQGHGLGASVTKS GNGIAESFRKQAEANLRLGDSASLIGKVSQTDTKIK GIDFKPQLSSSSLALQGDRLGASISRDVNRGVSDTL TKSISANVFRNDNHNLDASVFRSDVRQNNGFNFQK TGGMLDYSHANGHGLNAGLTRFSGIGNQANVGGY STLFRSNDGLTSLKANAGGSQWLSGPFANQRDYSF GLGLSHNAWRG 773 Sarcotoxin IIA Sarcophaga 294 MKSFVFFAACMAIIALSSLVQAYPQKLPVPIPPPTNP precursor peregrina PVAAFHNSVATNSKGGQDVSVKLAATNLGNKHVQP IAEVFAEGNTKGGNVLRGATVGVQGHGLGASVTKS QDGIAESFRKQAEANLRLGDSASLIGKVSQTDTKIK GIDFKPQLSSSSLALQGDRLGASISRDVNRGVSDTL TKSVSANLFRNDNHNLDASVFRSDVRQNNGFNFQK TGGMLDYSHANGHGLNAGLTRFSGIGNQATVGGY STLFRSNDGLTSLKANAGGSQWLSGPFANQRDYSF GLGLSHNAWRG 774 Scorpine Pandinus 94 MNSKLTALIFLGLIAIAYCGWINEEKIQKKIDERMGNT precursor imperator VLGGMAKAIVHKMAKNEFQCMANMDMLGNCEKHC QTSGEKGYCHGTKCKCGTPLSY 775 Secretogranin I Bos taurus 646 MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTH precursor (SgI) CIIEVLSNALLKSSAPPITPECRQVLKKNGKELKNEE (Chromogranin KSENENTRFEVRLLRDPADTSEAPGLSSREDSGEG B) (CgB) DAQVPTVADTESGGHSRERAGEPPGSQVAKEAKT [Contains: RYSKSEGQNREEEMVKYQKRERGEVGSEERLSEG GAWK peptide; PGKAQTAFLNQRNQTPAKKEELVSRYDTQSARGLE Secretolytin] KSHSRERSSQESGEETKSQENWPQELQRHPEGQE APGESEEDASPEVDKRHSRPRHHHGRSRPDRSSQ EGNPPLEEESHVGTGNSDEEKARHPAHFRALEEGA EYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQAL RRPSEESLEQENKRHGLSPDLNMAQGYSEESEEE RGPAPGPSYRARGGEAAAYSTLGQTDEKRFLGETH HRVQESQRDKARRRLPGELRNYLDYGEEKGEEAA RGKWQPQGDPRDADENREEARLRGKQYAPHHITE KRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGE EENGLTLNEKNFFPEYNYDWWEKKPFEEDVNWGY EKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFP DFYDSEEQMSPQHTAENEEEKAGQGVLTEEEEKEL ENLAAMDLELQKIAEKFSGTRRG 776 Similar to Mus 93 MKKLVLLSALVLLAYQVQTDPIQNTDEETNTEEQPG cryptdin-4 musculus EEDQAVSVSFGGQEGSALHEKLSRDLICLCRKRRC NRGELFYGTCAGPFLRCCRRRR 777 Similar to Mus 93 MKTLVLLSALILLAYQVQTDPIQNTDEETNTEEQPGE cryptdin-4 musculus DDQAVSVSFGGQEGSALHEKLSRDLICLCRNRRCN RGELFYGTCAGPFLRCCRRRR 778 Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTEEQAG cryptdin-4 musculus EEDQAVSVSFGDPEGSALHEKSSRDLICYCRKGGC NRGEQVYGTCSGRLLFCCRRRHRH 779 Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTEEQAG cryptdin-4 musculus EEDQAVSVSFGDPEGSALHEKSSRDLICYCRKGGC NRGEQVYGTCSGRLLLCCRRRHRH 780 Similar to Mus 95 MKTLVLLSALVLLAFQVQADPIQNTDEETNTEEQPG cryptdin-4 musculus EEDQAVSVSFGDPEGSALHEKSSRDLICYCRKGGC NRGEQVYGTCSGRLLFCCRRRHRH 781 Single WAP Mus 80 MKLLGLSLLAVTILLCCNMARPEIKKKNVFSKPGYCP motif protein 1 musculus EYRVPCPFVLIPKCRRDKGCKDALKCCFFYCQMRC precursor VDPWESPE (Elafin-like protein I) 782 Single WAP Mus 85 MWPNSILVLMTLLISSTLVTGGGVKGEEKRVCPPDY motif protein 2 musculus VRCIRQDDPQCYSDNDCGDQEICCFWQCGFKCVL precursor PVKDNSEEQIPQSKV (Elafin-like protein II) 783 Spingerin Pseudacan 25 HVDKKVADKVLLLKQLRIMRLLTRL thotermes spiniger 784 Styelin A Styela 20 GXFGKAFXSVSNFAKKHKTA (Fragment) clava 785 Styelin B Styela 20 GXFGPAFHSVSNFAKKHKTA (Fragment) clava 786 Styelin C Styela 80 MQMKATILIVLVALFMIQQSEAGWFGKAFRSVSNFY precursor clava KKHKTYIHAGLSAATLLGDMTDEEFQEFMQDIEQAR EEELLSRQ 787 Styelin D Styela 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSVGKFY precursor clava YKHKYYIKAAWQIGKHALGDMTDEEFQDFMKEVEQ AREEELQSRQ 788 Styelin E Styela 81 MQMKATILIVLVALFMIQQSEAGWLRKAAKSVGKFY precursor clava YKHKYYIKAAWKIGRHALGDMTDEEFQDFMKEVEQ AREEELQSRQ 789 T22H6.7 protein Caenorhabditis 195 MFRKLIIATFVLSLCDLANSVTICSSSSLLSTFTDPLC (ABF-6) elegans TSWCKVRFCSSGSCRSVMSGSDPTCECESCGFGS WFGSSSDSNSNQPVSGQYYAGGSGGEMATPNYG NNNGYNNGYNNGNNMRYNDNNGYNTNNGYRGQP TPGYGNSNSNFNSNQQYSYQQYYNNRNNQYGNS GYGNAGQAGQTGYPSGYQNLKKKR 790 tachycitin Tachypleus 98 MASSFMFAVVVLFISLAANVESYLAFRCGRYSPCLD precursor tridentatus DGPNVNLYSCCSFYNCHKCLARLENCPKGLHYNAY LKVCDWPSKAGCTSVNKECHLWKTGRK 791 Tachyplesin I Tachypleus 77 MKKLVIALCLMMVLAVMVEEAEAKWCFRVCYRGIC precursor tridentatus YRRCRGKRNEVRQYRDRGYDVRAIPEETFFTRQDE DEDDDEE 792 Tachyplesin II Tachypleus 77 MKKLVIALCLMMVLAVMVEEAEARWCFRVCYRGIC precursor tridentatus YRKCRGKRNEVRQYRDRGYDVRAIPDETFFTRQDE DEDDDEE 793 Tachystatin A2 Tachypleus 67 MKLQNTLILIGCLFLMGAMIGDAYSRCQLQGFNCVV precursor tridentatus RSYGLPTIPCCRGLTCRSYFPGSTYGRCQRY 794 Temporin A Rana 13 FLPLIGRVLSGIL temporaria 795 Temporin B Rana 61 MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPD precursor temporaria ERDVQVEKRLLPIVGNLLKSLLGK 796 Temporin C Rana 13 LLPILGNLLNGLL temporaria 797 Temporin D Rana 13 LLPIVGNLLNSLL temporaria 798 Temporin E Rana 13 VLPIIGNLLNSLL temporaria 799 Temporin F Rana 13 FLPLIGKVLSGIL temporaria 800 Temporin G Rana 61 MFTLKKSLLLLFFLGTINLSLCEEERDADEERRDDLE precursor temporaria ERDVEVEKRFFPVIGRILNGILGK 801 Temporin H Rana 58 MFTLKKSLLLLFFLGTINLSLCEEERNAEEERRDEPD precursor temporaria ERDVQVEKRLSPNLLKSLLGK 802 Temporin K Rana 10 LLPNLLKSLL temporaria 803 Temporin L Rana 13 FVQWFSKFLGRIL temporaria 804 Temporin-1CA Rana 13 FLPFLAKILTGVL clamitans 805 Temporin-1CB Rana 13 FLPLFASLIGKLL clamitans 806 Temporin-1CC Rana 13 FLPFLASLLTKVL clamitans 807 Temporin-1CD Rana 13 FLPFLASLLSKVL clamitans 808 Temporin-1CE Rana 13 FLPFLATLLSKVL clamitans 809 Temporin-1Ja Rana 13 ILPLVGNLLNDLL japonica 810 Temporin-1LA Rana 13 VLPLISMALGKLL luteiventris 811 Temporin-1LB Rana 14 NFLGTLINLAKKIM luteiventris 812 Temporin-1LC Rana 14 FLPILINLIHKGLL luteiventris 813 Temporin-1P Rana 13 FLPIVGKLLSGLL pipiens 814 Tenecin 1 Tenebrio 84 MKLTIFALVACFFILQIAAFPLEEAATAEEIEQGEHIRV precursor molitor KRVTCDILSVEAKGVKLNDAACAAHCLFRGRSGGY CNGKRVCVCR 815 Tenecin 3 Tenebrio 96 MKTFVICLILVVAVSAAPDHHDGHLGGHQTGHQGG precursor molitor QQGGHLGGQQGGHLGGHQGGQPGGHLGGHQGG IGGTGGQQHGQHGPGTGAGHQGGYKTHGH 816 Termicin Pseudacanthotermes 36 ACNFQSCWATCQAQHSIYFRRAFCDRSQCKCVFV spiniger RG 817 Testis defensin Mus 41 MKTLVLLSALFLLAFQVQADPIQNTDEETNTEVQPQ (Fragment) musculus EEDQA 818 Testis defensin Mus 40 MKTLVLLSPSSCWPSRSRLILSKTQMKRLKLRSSQR (Fragment) musculus KRTR 819 Testis-specific Mus 83 MRLALLLLAILVATELVVSGKNPILQCMGNRGFCRS beta-defensin- musculus SCKKSEQAYFYCRTFQMCCLQSYVRISLTGVDDNT like protein NWSYEKHWPRIP 820 Thanatin Podisus 21 GSKKPVPIIYCNRRTGKCQRM maculiventris 821 Theta Defensin 1 Macaca 18 GFCRCLCRRGVCRCICTR mulatta 822 theta defensin Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQ 1a precursor mulatta PGTDDQGMAHSFTWPENAALPLSESAKGLRCICTR GFCRLL 823 theta defensin Macaca 76 MRTFALLTAMLLLVALHAQAEARQARADEAAAQQQ 1b precursor mulatta PGADDQGMAHSFTRPENAALPLSESARGLRCLCRR GVCQLL 824 theta defensin-1 Macaca 18 RCICTRGFCRCLCRRGVC mulatta 825 Tigerinin-1 Hoplobatrachus 11 FCTMIPIPRCY tigerinus 826 Tigerinin-2 Hoplobatrachus 12 RVCFAIPLPICH tigerinus 827 Tigerinin-3 Hoplobatrachus 12 RVCYAIPLPICY tigerinus 828 Tigerinin-4 Hoplobatrachus 11 RVCYAIPLPIC tigerinus 829 tracheal Bos taurus 64 MRLHHLLLALLFLVLSASSGFTQGVGNPVSCVRNK antimicrobial GICVPIRCPGNMKQIGTCVGRAVKCCRKK peptide 830 Tracheal Bos taurus 64 MRLHHLLLALLFLVLSAWSGFTQGVGNPVSCVRNK antimicrobial GICVPIRCPGSMKQIGTCVGRAVKCCRKK peptide precursor (TAP) 831 Xenopsin Xenopus 81 MYKGIFLCVLLAVICANSLATPSSDADEDNDEVERY precursor laevis VRGWASKIGQTLGKIAKVGLKELIQPKREAMLRSAE [Contains: AQGKRPWIL Xenopsin precursor fragment (XPF); Xenopsin] Plant Antimicrobial Peptides Organism Protein Name Name Length Sequence 832 22K antifungal Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGRQLNRGESWRI protein TAPAGTTAARIWARTGCQFDASGRGSCRTGDCGG VVQCTGYGRAPNTLAEYALKQFNNLDFFDISLIDGF NVPMSFLPDGGSGCSRGPRCAVDVNARCPAELRQ DGVCNNACPVFKKDEYCCVGSAANNCHPTNYSRY FKGQCPDAYSYPKDDATSTFTCPAGTNYKVVFCP 833 AC- Amaranthus 29 VGECVRGRCPSGMCCSQFGYCGKGPKYCG AMP1 =ANTIMICROBIAL caudatus peptide 834 Alpha- Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGRQLNRGESWRI amylase/trypsin TAPAGTTAARIWARTGCQFDASGRGSCRTGDCGG inhibitor VVQCTGYGRAPNTLAEYALKQFNNLDFFDISILDGF (Antifungal NVPYSFLPDGGSGCSRGPRCAVDVNARCPAELRQ protein) DGVCNNACPVFKKDEYCCVGSAANNCHPTNYSRY FKGQCPDAYSYPKDDATSTFTCPAGTNYKVVFCP 835 Alpha-basrubrin Basella 20 GADFQECMKEHSQKQHQHQG (Fragment) alba 836 antifungal 25K Linum 37 ARFDIQNKCPYTVWAASVPVGGGRQLNSGQTWXID protein usitatissimum AP 837 antifungal 27K Diospyros 30 ATFDIQNKXTYTVWAAAWAPSYPGGXKQLD protein texana 838 antifungal 2S Raphanus 20 PQGPQQRPPLLQQCCNNLLQ storage albumin sativus large chain 839 antifungal 2S Raphanus 30 PAGPFRIPRCRREFQQAQHLRACQQWLHRQ storage albumin sativus small chain 840 Antifungal Phytolacca 38 AGCIKNGGRCNASAGPPYCCSSYCFQIAGQSYGVC Peptide americana KNR 841 Antifungal Eucommia 41 QTCASRCPRPCNAGLCCSIYGYCGSGNAYCGAGN peptide 1 ulmoides CRCQCRG (EAFP1) 842 Antifungal Eucommia 41 QTCASRCPRPCNAGLCCSIYGYCGSGAAYCGAGN peptide 2 ulmoides CRCQCRG (EAFP2) 843 Antifungal Gastrodia 171 MAASASTAVILFFAVTTMMSLSAIPAFASDRLNSDH protein elata QLDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVWAS GTNGKASNCFLKMQNDGNLVIYSGSRAIWASNTNR QKGNYYLILQRDRNVVIYDNSNNAIWATHTNVGNAE ITVIPHSNGTAAASGAAQNKVNELYISMY 844 Antifungal Gastrodia 169 MASPASSAVIFLFAVAALMSLLAMPALAASQLNAGQ protein elata TLGTGQSLAQGPDQFVIQNDCNLVLYDSNRVVWAS GTNGKASGCVLRMQRDGNLVIYSGSRVIWASNTNR RDDNYYLLLQRDRNVVIYDSSNNAIWATGTNVGNA AITVIPHSNGTAAASGAAQNKVNEYLRP 845 Antifungal Ipomoea nil 92 MKFCTMFLVVLALASLLLTPSTIMAQQCGSQARGRL protein CGNGLCCSQWGYCGSTAAYCGAGCQSQCKSTAA SATDTTTTANQSTAKSDPAGGAN 846 Antifungal Capsicum 85 MKFQVVILVLFALLLTRTSAQNCGRQAGRRVCANRL protein annuum CCSQFGFCGTTREYCGAGCQSNCRRYATDTTGEG ENVNNDEHKNNGGPN 847 Antifungal Ipomoea nil 91 MKYCTMFIVLLGLGSLLLTPTTIMAQQCGRQASGRL protein CGNGLCCSQWGYCGSTAAYCGAGCQSQCKSTAA SSTTTTTANQSTAKSDPAGGAN 848 antifungal Sinapis 25 QKLCERPSGTWSGVCGNNNACKNQC protein 1 alba 849 antifungal Brassica 30 QKLCERPSGTWSGVCGNNNACKNQCINLEK protein 1 napus 850 antifungal Arabidopsis 27 QKLCERPSGTWSGVCGNSNACKNQCIN protein 1 thaliana 851 Antifungal Raphanus 51 XKLCERPSGTWSGVCGNNNACKNQCINLEKARHG Protein 1 sativus SCNYVFPAHKCICYFPC 852 Antifungal Malva 15 VAGPFRIPPLRREFQ protein 1 large parviflora subunit (CW-1) (Fragment) 853 Anti-fungal Phytolacca 65 MAKVSSAYLKFALVMILLLSVISAVMSAGCIKNGGRC protein 1 americana NASAGPPYCCSSYCFQIAGQSYGVCKNR precursor (PAFP-S) 854 Antifungal Malva 16 PAGPFRIPPRXRXEFQ protein 1 small parviflora subunit (CW-1) (Fragment) 855 antifungal Sinapis 26 QKLCQRPSGTWSGVCGNNNACRNQCI protein 2 alba 856 Antifungal Malva 20 PEDPQRRYQEXQREXRXQQE protein 2 large parviflora subunit (CW-2) (Fragment) 857 Antifungal Malva 15 PEDPQRRYQEEQRRE protein 3 (CW- parviflora 3) (Fragment) 858 Antifungal Malva 37 DRQIDMEEQQLEKLNKQDRXPGLRYAAKQQMXTX protein 4 (CW- parviflora RMG 4) (Fragment) 859 Antifungal Malva 38 ITCGQVTSQVAGCLSYLQRGGAPAPXXXXGIRNLXX protein 5 (CW- parviflora MA 5) (Fragment) 860 Antifungal Beta 46 AICKKPSKFFKGACGRDADCEKACDQENWPGGVC protein AX1 vulgaris VPFLRCECQRSC 861 Antifungal Beta 46 ATCRKPSMYFSGACFSDTNCQKACNREDWPNGKC protein AX2 vulgaris LVGFKCECQRPC 862 Antifungal Gastrodia 129 SDRLNSGHQLDTGGSLAEGGYLFIIQNDCNLVLYDN protein GAFP-1 elata NRAVWASGTNGKASGCVLKMQNDGNLVIYSGSRAI (Fragment) WASNTNRQNGNYYLILQRDRNVVIYDNSNNAIWAT HTNVGNAEITVIPHSNGTAAASG 863 Antifungal Medicago 72 MEKKSLAGLCFLFLVLFVAQEIVVTEARTCENLADKY protein sativa RGPCFSGCDTHCTTKENAVSGRCRDDFRCWCTKRC precursor 864 Antifungal Gastrodia 178 MLEWGDGVFCGGCVGYLRGDSVECGNCSDRLNS protein elata GHQLDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVW precursor ASGTNGKASGCVLKMQNDGNLVIYSGSRAIWASNT NRQNGNYYLILQRDRNVVIYDNSNNAIWATHTNVG NAEITAIPHSNGTAAASGAAQNKVNELYISMYSRSK RIAG 865 Antifungal Hordeum 44 ATITVVNRCSYTVWPGALPGGGVRLDPGQRWALN protein R vulgare MPAGTAGAAV (Fragment) 866 Antifungal Hordeum 37 ATFTVINKCQYTVWAAAVPAGGGQKLDAGQTWSIX protein S vulgare XP (Fragment) 867 Antifungal Arabidopsis 80 MAKSATIITFLFAALVLFAAFEAPTMVEAQKLCEKPS protein-like thaliana GTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPA HKCICYVPC 868 Antimicrobial Pisum 60 ALSFLFLFLFVAQEIVVTEANTCEHLADTYRGVCFTD defensin sativum ASCDDHCKNKAHLISGTCHNFKC peptide DRR230-c (Fragment) 869 Antimicrobial Macadamia 76 SAFTVWSGPGCNNRAERYSKCGCSAIHQKGGYDF Peptide 1 integrifolia SYTGQTAALYNQAGCSGVAHTRFGSSARACNPFG WKSIFIQC 870 Antimicrobial Mesembryanthemum 64 MAKVSSSLLKFAIVLILVLSMSAIISAKCIKNGKGCRE peptide 1 crystallinum DQGPPFCCSGFCYRQVGWARGYCKNR precursor 871 Antimicrobial Macadamia 102 MASTKLFFSVITVMMLIAMASEMVNGSAFTVWSGP peptide 1 integrifolia GCNNRAERYSKCGCSAIHQKGGYDFSYTGQTAALY precursor NQAGCSGVAHTRFGSSARACNPFGWKSIFIQC (AMP1) 872 Antimicrobial Mirabilis 61 LPVAFLKFAIVLILFIAMSAMIEAQCIGNGGRCNENVG peptide 1 jalapa PPYCCSGFCLRQPGQGYGYCKNR precursor (AMP1) (MJ- AMP1) (Fragment) 873 Antimicrobial Amaranthus 30 VGECVRGRCPSGMCCSQFGYCGKGPKYCGR Peptide 2 caudatus 874 Antimicrobial Mirabilis 63 MAKVPIAFLKFVIVLILFIAMSGMIEACIGNGGRCNEN peptide 2 jalapa VGPPYCCSGFCLRQPNQGYGVCRNR precursor (AMP2) (MJ- AMP2) 875 Antimicrobial Spinacia 22 XTCESPSHKFKGPCATNRNCES peptide D1 (so- oleracea D1) (Defensin D1) (Fragment) 876 Antimicrobial Spinacia 52 GIFSSRKCKTPSKTFKGICTRDSNCDTSCRYEGYPA peptide D2 (So- oleracea GDCKGIRRRCMCSKPC D2) (Defensin D2) (Fragment) 877 Antimicrobial Spinacia 25 GIFSSRKCKTVSKTFRGICTRNANC peptide D3 (So- oleracea D3) (Defensin D3) (Fragment) 878 Antimicrobial Spinacia 23 MFFSSKKCKTVSKTFRGPCVRNA peptide D4 (So- oleracea D4) (Defensin D4) (Fragment) 879 Antimicrobial Spinacia 24 MFFSSKKCKTVXKTFRGPCVRNAN peptide D5 (So- oleracea D5) (Defensin D5) (Fragment) 880 Antimicrobial Spinacia 24 GIFSNMYXRTPAGYFRGPXGYXXN peptide D6 (So- oleracea D6) (Defensin D6) (Fragment) 881 Antimicrobial Spinacia 38 GIFSSRKCKTPSKTFKGYCTRDSNCDTSCRYEGYP peptide D7 (So- oleracea AGD D7) (Defensin D7) (Fragment) 882 Antimicrobial Zea mays 33 RSGRGECRRQCLRRHEGQPWETQECMRRCRRRG peptide MBP-1 883 Antimicrobial Capsella 120 MASKTLILLGLFAILLVVSEVSAARESGMVKPESEET peptide shep- bursa- VQPEGYGGHGGHGGHGGHGGHGGHGHGGGGHG GRP pastoris LDGYHGGHGGHGGGYNGGGGHGGHGGGYNGGG HHGGGGHGLNEPVQTQPGV 884 Antimicrobial Impatiens 333 MVQKGVVFGVLLILFICSTLTSADSKPNPTKEEEPAK peptides balsamina KPDEVSVKSGGPEVSEDQYRHRCCAWGPGRKYCK precursor (IB- RWCANAEEAAAAIPEASEELAQEEAPVYSEDQWGR AMP) RCCGWGPGRRYCVRWCQNAEEAAAAIPEATEKAQ [Contains: EAPVYSEDQWGRRCCGWGPGRRYCVRWCQNAE Basic peptide EAAAAVAIPEASEKAQEGPVYSEDQWGRRCCGWG AMP3 (IB- PGRRYCVRWCSNAADEVATPEDVEPGQYGRRCC AMP3); Basic NWGPGRRYCKRWCHNAAEEATLKAFEEEAAREQP peptide AMP1-1 VYSEDQWGRRCCGWGPGRRYCRRWCQSAEEAA (IB-AMP1-1); AFQAGEVTASLMLIMFKACPCMGPVPSV Basic peptide AMP1-2 (IB- AMP1-2); Basic peptide AMP1-3 (IB-AMP1-3); Basic peptide A 885 Antimicrobial Allium cepa 132 MVRVVSLLAASTFILLIMIISSPYANSQNICPRVNRIVT protein Ace- PCVAYGLGRAPIAPCCRALNDLRFVNTRNLRRAAC AMP1 RCLVGVVNRNPGLRRNPRFQNIPRDCRNTFVRPFW precursor WRPRIQCGRINLTDKLIYLDAEE 886 Antimicrobial Ipomoea nil 41 QQCGRQASGRLCGNRLCCSQWGYCGSTASYCGA protein PN- GCQSQCRS AMP (PN- AMP1/PN- AMP2) 887 antimicrobial Amaranthus 86 MVNMKCVALIVIVMMAFMMVDPSMGVGECVRGRC protein hypochondriacus PSGMCCSQFGYCGKGPKYCGRASTTVDHQADVAA precursor TKTAKNPTDAKLAGAGSP 888 Antimicrobial Phytolacca 37 ACIKNGGRCVASGGPPYCCSNYCLQIAGQSYGVCK seed protein americana KH (Fragment) 889 avematin Avena 26 TTITVVNKCSYTVWPGALPGGGVVLD sativa 890 Basal layer Zea mays 93 MAKFFNYTIIQGLLMLSMVLLASCAIHAHIISGETEEV antifungal SNTGSPTVMVTMGANRKIIEDNKNLLCYLRALEYCC peptide ARTRQCYDDIKKCLEHCRG precursor 891 Basal layer Zea mays 96 MVKILDHISIRGFFLLFMVLVASFVGHAQIIRGETKED antifungal NDTKSMTMTTMRPGSYVTSMDEKSSLCFEDIKTLW peptide YICRTTYHLYRTLKDCLSHCNSM precursor 892 Basal layer Zea mays 95 MVKSLDHITIRGLFLLFMFLVASFVGHAQIIRGETKEN antifungal KDTNSMTMTTRPGSYVISMDEKSSLCFLDPRTLWYI peptide CKITYRLFRTLKDCLEFCHSI precursor 893 Basal layer Zea mays 73 MVLLASCVIHAHIISGEIEDVSNTRSPTMMGANRKIIG antifungal DNKNLLCYLKALEYCCERTKQCYDDIKKCLEHCHS peptide precursor 894 Beta-basrubin Basella 16 KIMAKPSKFYEQLRGR (Fragment) alba 895 CBP20 Nicotiana 208 GKLSTLLLVLILYFIAAGANAQQCGRQRGGALCSGN (Fragment) tabacum LCCSQFGWCGSTPEYCSPSQGCQSQCSGGGGGG GGGGGGGAQNVRATYHIYNPQNVGWDLYAVSAYC STWDGNKPLAWRRKYGWTAFCGPVGPRGRDSCG KCLRVTNTGTGAQTTVRIVDQCSNGGLDLDVNVFR QLDTDGRGNQRGHLIVNYEFVNCGDNMNVLLSPVD KE 896 CBP20 Nicotiana 211 MGKLSTLLFALVLYVIAAGANAQQCGRQRGGALCS preproprotein tabacum GNLCCIQFGWCGSTQEYCSPSQGCQSQCSGGGG GGGGGGGGGGAAQNVRATYHIYNPQNVGWDLYA VSAYCSTWDGNKPLAWRRKYGWTAFCGPVGPRG RDSCGKCLRVTNTGTGAQTTVRIVDQCSNGGLDLD VNVFRQLDTDGRGNQRGHLIVNYEFVNCGDNMNV LVSPVDKE 897 chitinase (EC Nicotiana 378 MANSVTLFSIIFSCFLLRQLVCTNSQNVIKGGYWFKN 3.2.1.14)/ tabacum SGLALNNIDSTLFTHLFCAFADLNPQSNQLIISPENQ lysozyme (EC DSFSQFTSTVQRKNPSVKTFLSIAGGRADTTAYGIM 3.2.1.17) PZ ARQPNSRKSFIDSSIRLARQFGFHGLDLDWEYPLSA precursor, TDMTNLGILLNEWRTAINMEARNSGRAALLLTAAVS pathogenesis- YSPRVNGLNYPVESVARNLNWINLMAYDFYGPNWS related PSQTNSHAQLFDPVNHISGSDGINAWIQAGVPTKKL VLGIPFYGYAWRLVNPNIHDLRAPAAGKSNVGAVD DGSMTYNRIRDYIVQSRATTVYNATIVGDYCYSGSN WISYDDTQSVRNKVNYVKGRGLLGYFAWHVAGDQ NWGLSRTASQTWGVSSQEMK 898 chitinase (EC Zea mays 280 MANAPRILALGLLALLCAAAGPAAAQNCGCQPNFC 3.2.1.14) A CSKFGYCGTTDAYCGDGCQSGPCRSGGGGGGGG GGGGGGSGGANVANVVTDAFFNGIKNQAGSGCEG KNFYTRSAFLSAVNAYPGFAHGGTEVEGKREIAAFF AHVTHETGHFCYISEINKSNAYCDASNRQWPCAAG QKYYGRGPLQISWNYNYGPAGRDIGFNGLADPNRV AQDAVIAFKTALWFWMNNVHRVMPQGFGATIRAIN GALECNGNNPAQMNARVGYYKQYCQQLRVDPGP NLIC 899 chitinase (EC Zea mays 268 QLVALGLALLCAVAGPAAAQNCGCQPNVCCSKFGY 3.2.1.14) CGTTDEYCGDGCQSGPCRSGRGGGGSGGGGANV precursor ASVVTSSFFNGIKNQAGSGCEGKNFYTRSAFLSAVK GYPGFAHGGSQVQGKREIAAFFAHATHETGHFCYI SEINKSNAYCDPTKRQWPCAAGQKYYGRGPLQISW NYNYGPAGRAIGFDGLGDPGRVARDAVVAFKAALW FWMNSVHGVVPQGFGATTRAMQRALECGGNNPA QMNARVGYYRQYCRQLGVDPGPNLTC 900 Chitinase, class V Nicotiana 377 MANSVTLFAIIFSCFLLQQLVCTNSQNVKGGYWFKD tabacum SGLALNNIDSTLFTHLFCAFADLNPQLNQLIISPENQ DSFRQFTSTVQRKNPSVKTFLSIAGGRANSTAYGIM ARQPNSRKSFIDSSIRLARQLGFHGLDLDWEYPLSA ADMTNLGTLLNEWRTAINTEARNSGRAALLLTAAVS NSPRVNGLNYPVESLARNLDWINLMAYDFYGPNWS PSQTNSHAQLFDPVNHVSGSDGINAWIQAGVPTKK LVLGIPFYGYAWRLVNANIHGLRAPAAGKSNVGAVD DGSMTYNRIRDYIVESRATTVYNATIVGDYCYSGSN WISYDDTQTVRNKVNYVKGRGLLGYFAWHVAGDQ NWGLSRTASQTWGVSFQEMK 901 Chitin-binding Hydrangea 15 NSMERVEELRKKLQD protein HM30 macrophylla (Fragment) 902 Chitin-binding Hordeum 52 ATYHYYRPAQNNWDLGAPAVSAYCATWDASKYGW protein N, CBP vulgare TAFIVDQCANGGLDLDWN N (Fragments) 903 Circulin A Chassalia 30 GIPCGESCVWIPCISAALGCSCKNKVCYRN (CIRA) parviflora 904 Circulin B Chassalia 31 GVIPCGESCVFIPCISTLLGCSCKNKVCYRN (CIRB) parviflora 905 Cyclopsychotride Psychotria 31 SIPCGESCVFIPCTVTALLGCSCKSKVCYKN A (CPT) longipes 906 Cysteine-rich Brassica 27 QKLCERPSGTWSGVCGNNNACKNQCIN antifungal rapa protein 1 (AFP1) (Fragment) 907 Cysteine-rich Sinapis 51 QKLCERPSGWSGVCGNNNACKNQCINLEKARHG antifungal alba SCNYVFPAHKCICYFPC protein 1 (AFP1) (M1) 908 Cysteine-rich Raphanus 80 MAKFASIIALLFAALVLFAAFEAPTMVEAQKLCERPS antifungal sativus GTWSGVCGNNNACKNQCINLEKARHGSCNYVFPA protein 1 HKCICYFPC precursor (AFP1) 909 Cysteine-rich Arabidopsis 80 MAKSATIVTLFFAALVFFAALEAPMVVEAQKLCERP antifungal thaliana SGTWSGVCGNSNACKNQCINLEKARHGSCNYVFP protein 1 AHKCICYFPC precursor (AFP1) (Anther- specific protein S18 homolog) 910 Cysteine-rich Brassica 23 QKLCERPSGTWSGVCGNNNACKN antifungal napus protein 2 (AFP2) (Fragment) 911 Cysteine-rich Brassica 27 QKLCERPSGTXSGVCGNNNACKNQCIR antifungal rapa protein 2 (AFP2) (Fragment) 912 Cysteine-rich Raphanus 80 MAKFASIIVLLFVALVVFAAFEEPTMVEAQKLCQRPS antifungal sativus GTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPA protein 2 HKCICYFPC precursor (AFP2) 913 Cysteine-rich Sinapis 51 QKLCQRPSGTWSGVCGNNNACRNQCINLEKARHG antifungal alba SCNYVFPAHKCICYFPC protein 2A (AFP2A) (M2A) 914 Cysteine-rich Sinapis 52 QKLCARPSGTWSSGNCRNNNACRNFCIKLEKSRH antifungal alba GSCNIPFPSNKCICYFPC protein 2B (AFP2B) (M2B) 915 Cysteine-rich Brassica 79 MAKFASIITLLFAALVVFAAFEAPTMVEAKLCERSSG antifungal napus TWSGVCGNNNACKNQCIRLEGAQHGSCNYVFPAH protein 3 KCICYFPC precursor (AFP3) 916 Cysteine-rich Raphanus 79 MAKFASIVALLFAALVVFAAFEAPTVVEAKLCERSSG antifungal sativus TWSGVCGNNNACKNQCIRLEGAQHGSCNYVFPAH protein 3 KCICYFPC precursor (AFP3) 917 Cysteine-rich Raphanus 80 MAKFVSIITLLFVALVLFAAFEAPTMVEAQKLCERSS antifungal sativus GTWSGVCGNNNACKNQCINLEGARHGSCNYIFPYH protein 4 RCICYFPC precursor (AFP4) 918 Defense-related Pisum 46 KTCEHLADTYRGVCFTNASCDDHCKNKAHLISGTC peptide 1 sativum HNWKCFCTQNC (Defensin 1) (Antifungal protein Psd1) 919 Defense-related Pisum 47 KTCENLSGTFKGPCIPDGNCNKHCRNNEHLLSGRC peptide 2 sativum RDDFRCWCTNRC (Defensin 2) (Antifungal protein Psd2) 920 defensin Capsicum 75 MAGFSKVIATIFLMMMLVFATDMMAEAKICEALSGN annuum FKGLCLSSRDCGNVCRREGFTSGVCRGFPLKCFCR KPGA 921 Defensin Brassica 80 MAKFVSIITLFFAALVLFAAFEAPTMVKAQKLCERSS rapa GTWSGVCGNNNACKNQCINLEGARHGSCNYVFPY HRCICYFPC 922 Defensin Helianthus 108 MAKISVAFNAFLLLLFVLAISEIGSVKGELCEKASQT annuus WSGTCGKTKHCDDQCKSWEGAAHGACHVRDGKH MCFCYFNCSKAQKLAQDKLRAEELAKEKIEPEKATA KP 923 Defensin Helianthus 41 SHRFQGTCLSDTNCANVCHSERFSGGKCRGFRRR (Fragment) annuus CFCTTHC 924 defensin 1 Triticum 82 MASTRRMAAAPAVLLLLLLLVATEMGTMKTAEARTC precursor aestivum LSQSHKFKGTCLSNSNCAAVCRTENFPDGECNTHL VERKCYCKRTC 925 defensin AFP1 Heuchera 54 DGVKLCDVPSGTWSGHCGSSSKCSQQCKDREHFA sanguinea YGGACHYQFPSVKCFCKRQC 926 defensin AMP1 Dahlia 50 ELCEKASKTWSGNCGNTGHCDNQCKSWEGAAHG merckii ACHVRNGKHMCFCYFNC 927 defensin AMP1 Aesculus 50 LCNERPSQTWSGNCGNTAHCDKQCQDWEKASHG hippocastanum ACHKRENHWKCFCYFNC 928 defensin AMP1 Clitoria 49 NLCERASLTWTGNCGNTGHCDTQCRNWESAKHG ternatea ACHKRGNWKCFCYFNC 929 defensin AMP2 Dahlia 20 EVCEKASKTWSGNCGNTGHC merckii 930 Defensin CUA1 Helianthus 42 LSHSFKGTCLSDTNCANVCHSERFSGGKCRGFRR (Fragment) annuus RCFCTTHC 931 Defensin Elaeis 77 MEHSRRMLPAILLLLFLLMPSEMGTKVAEARTCESQ EGAD1 guineensis SHKFQGTCLRESNCANVCQTEGFQGGVCRGVRRR CFCTRLC 932 Defensin J1-1 Capsicum 75 MAGFSKVVATIFLMMLLVFATDMMAEAKICEALSGN precursor annuum FKGLCLSSRDCGNVCRREGFTDGSCIGFRLQCFCT KPCA 933 Defensin J1-2 Capsicum 74 MAGFSKVIATIFLMMMLVFATGMVAEARTCESQSH precursor annuum RFKGLCFSKSNCGSVCHTEGFNGGHCRGFRRRCF CTRHC 934 Defensin Brassica 80 MAKVASIVALLFPALVIFAAFEAPTMVEAQKLCERPS precursor oleracea GTWSGVCGNNNACKNQCIRLEKARHGSCNYVFPA HKCICYFPC 935 Defensin Prunus 79 MERSMRLFSTAFVFFLLLAAAGMMMGPMVAEARTC protein 1 persica ESQSNRFKGTCVSTSNCASVCQTEGFPGGHCRGF RRRCFCTKHC 936 Endochitinase Zea mays 280 MANAPRILALGLLALLCAAAGPAAAQNCGCQPNFC A precursor (EC CSKFGYCGTTDAYCGDGCQSGPCRSGGGGGGGG 3.2.1.14) (Seed GGGGGGSGGANVANVVTDAFFNGIKNQAGSGCEG chitinase A) KNFYTRSAFLSAVNAYPGFAHGGTEVEGKREIAAFF AHVTHETGHFCYISEINKSNAYCDASNRQWPCAAG QKYYGRGPLQISWNYNYGPAGRDIGFNGLADPNRV AQDAVIAFKTALWFWMNNVHGVMPQGFGATIRAIN GALECNGNNPAQMNARVGYYKQYCQQLRVDPGP NLIC 937 Endochitinase Zea mays 269 PQLVALGLALLCAVAGPAAAQNCGCQPNVCCSKFG B precursor (EC YCGTTDEYCGDGCQSGPCRSGRGGGGSGGGGAN 3.2.1.14) (Seed VASVVTSSFFNGIKNQAGSGCEGKNFYTRSAFLSAV chitinase B) KGYPGFAHGGSQVQGKREIAAFFAHATHETGHFCY (Fragment) ISEINKSNAYCDPTKRQWPCAAGQKYYGRGPLQIS WNYNYGPAGRAIGFDGLGDPGRVARDAVVAFKAAL WFWMNSVHGVVPQGFGATTRAMQRALECGGNNP AQMNARVGYYRQYCRQLGVDPGPNLTC 938 Fabatin-1 Vicia faba 47 LLGRCKVKSNRFHGPCLTDTHCSTVCRGEGYKGG DCHGLRRRCMCLC 939 Fabatin-2 Vicia faba 47 LLGRCKVKSNRFNGPCLTDTHCSTVCRGEGYKGG DCHGLRRRCMCLC 940 Floral defensin- Petunia × 103 MARSICFFAVAILALMLFAAYDAEAATCKAECPTWD like protein 1 hybrida SVCINKKPCVACCKKAKFSDGHCSKILRRCLCTKEC VFEKTEATQTETFTKDVNTLAEALLEADMMV 941 Floral defensin- Petunia × 101 MARSICFFAVAILALMLFAAYETEAGTCKAECPTWE like protein 2 hybrida GICINKAPCVKCCKAQPEKFTDGHCSKILPRCLCTK PCATEEATATLANEVKTMAEALVEEDMME 942 Flower-specific Helianthus 78 MKSSMKMFAALLLVVMCLLANEMGGPLVVEARTCE gamma-thionin annuus SQSHKFKGTCLSDTNCANVCHSERFSGGKCRGFR precursor RRCFCTTHC (Defensin SD2) 943 Gamma-thionin Arabidopsis 77 MKLSMRLISAVLIMFMIFVATGMGPVTVEARTCESQ homolog thaliana SHRFKGTCVSASNCANVCHNEGFVGGNCRGFRRR At2g02100 CFCTRHC precursor 944 Gamma-thionin Arabidopsis 77 MKFSMRLISAVLFLVMIFVATGMGPVTVEARTCASQ homolog thaliana SQRFKGKCVSDTNCENVCHNEGFPGGDCRGFRRR At2g02120 CFCTRNC precursor 945 Gamma-thionin Arabidopsis 77 MKLSVRFISAALLLFMVFIATGMGPVTVEARTCESKS homolog thaliana HRFKGPCVSTHNCANVCHNEGFGGGKCRGFRRRC At2g02130 YCTRHC precursor 946 Gamma-thionin Arabidopsis 73 MKLSLRLISALLMSVMLLFATGMGPVEARTCESPSN homolog thaliana KFQGVCLNSQSCAKACPSEGFSGGRCSSLRCYCS At2g02140 KAC precursor 947 Gamma- Eutrema 80 MAKFASIIALLFAALVLFSAFEAPSMVEAQKLCEKSS thionin1 wasabi GTWSGVCGNNNACKNQCINLEGARHGSCNYIFPYH precursor RCICYFPC 948 gamma-thionin- Lycopersicon 105 MARSIFFMAFLVLAMMLFVTYEVEAQQICKAPSQTF like protein esculentum PGLCFMDSSCRKYCIKEKFTGGHCSKLQRKCLCTK precursor PCVFDKISSEVKATLGEEAKTLSEVVLEEEIMME 949 Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTMMSLSAIPAFASDRLNSGH MGM protein elata QLDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVWAS GTNGKASGCMLKMQNDGNLVIYSGSRAIWASNTNR QNGNYYLILQRDRNVVIYDNSNNAIWATHTNVGNAE ITVIPHSNGTAAASGAAQNKVNELYISMY 950 Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTMMSLSAIPAFASDRLNSGH MNF protein elata QLDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVWAS GTNGKASNCFLKMQNDGNLVIYSGSRAIWASNTNR QNGNYYLILQRDRNVVIYDNSNNAIWATHTNVGNAE ITVIPHSNGTAAASGAAQNKVNELYISMY 951 Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTVMSLSAIPAFASDRLNSGHQ VGM protein elata LDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVWASG TNGKASGCMLKMQNDGNLVIYSGSRAIWASNTNRQ NGNYYLILQRDRNVVIYDNSNNAIWATHTNVGNAEI TVIPHSNGTAAASGAAQNKVNELYISMY 952 Gastrodianin- Gastrodia 171 MAASASTAVILFFAVTTVMSLSAIPAFASDRLNSGHQ VNF protein elata LDTGGSLAQGGYLFIIQNDCNLVLYDNNRAVWASG TNGKASNCFLKMQNDGNLVIYSGSRAIWASNTNRQ NGNYYLILQRDRNVVIYDNSNNAIWATHTNVGNAEI TVIPHSNGTAAASGAAQNKVNELYISMY 953 Genomic DNA, Arabidopsis 73 MENKFFAAFFLLLVLFSSQEIIGGEGRTCQSKSHHF chromosome 5, thaliana KYMCTSNHNCAIVCRNEGFSGGRCHGFHRRCYCT P1 clone:MBK5 RLC 954 Ginkbilobin Ginkgo 40 ANTAFVSSAHNTQKIPAGAPFNRNLRAMLADLRQN (GNL) biloba AAFAG (Fragment) 955 Hevein Hevea 204 MNIFIVVLLCLTGVAIAEQCGRQAGGKLCPNNLCCS precursor brasiliensis QWGWCGSTDEYCSPDHNCQSNCKDSGEGVGGG (Major hevein) SASNVLATYHLYNSQDHGWDLNAASAYCSTWDAN [Contains: KPYSWRSKYGWTAFCGPVGAHGQSSCGKCLSVTN Hevein TGTGAKTTVRIVDQCSNGGLDLDVNVFRQLDTDGK (Allergen Hev b GYERGHITVNYQFVDCGDSFNPLFSVMKSSVIN 6); Win-like protein] 956 hevein-like Euonymus 320 MKYLWVFIVFSIAVLSHACSAQQCGRQAGNRRCAN antimicrobial europaeus NLCCSQYGYCGRTNEYCCTSQGCQSQCRRCGVR peptide TVGEIVVGDIGGIISKGMFNNILKHRDDDACEGKGFY TYEAFVAAARSFPAFGSTGDDATRKREIAAFLAQTS HETSAGWPSAPDGPYAWGYCFVRERNPPSKYCDT TTPCPKSYYGRGPIQLTWNYNYEQAGRAIGADLLN NPDLVATDAVISFKTAIWFWMTAQSSKPSCHDVITG SWRPSASDNSVCHVPDYAVVTNIISGEIEYGKSRNP QVEDRIEFFKRYCQILGVSPGKCYEERTFVSGLMME TI 957 hevein-like Euonymus 305 MKYLWVFIVFSIAVLSLACSAQQCGRQAGNRRCPN antimicrobial europaeus NLCCSQFGYCGRTNEYCCTGFGCQSNCRRCGVRT peptide VGEDVVGDIGGIISKGMFNNILKHRDDDACEGKGFY TYEAFVAAARSFPAFGSTGDDTTRKREIAAFLAQTS HETSGGRPSAPDGPYAWGYCFVKERNPPSKYCDTI TPCPKSYYGRGPLQLTWNYNYAQAGRAIGVDLLNN PDLVATDAVTSFKTAIWFWMTAHSSKPSCHDVITGS WRPSASDNSVRHVPDYAVVTNIINGEIEYGKSRNPQ VEDRIEFFKRYCQILGVSPGKF 958 Leaf-specific Hordeum 137 MAPSKSIKSVVICVLILGLVLEQVQVEGKSCCKDTLA thionin vulgare RNCYNTCHFAGGSRPVCAGACRCKIISGPKCPSDY precursor PKLNLLPESGEPDVTQYCTIGCRNSVCDNMDNVFR (Clone DB4) GQEMKFDMGLCSNACARFCNDGAVIQSVEA 959 Lectin-like Gastrodia 111 QSSPGILLNQPASMASPASSAVIFFFAVAALMSLLA protein elata MPALAASQLNAGQTLGTGQSLAQGPNQFIIQNDCN (Fragment) LVLYASNKAVWATGTNGKASGCVLRMQRDGNLVIY SGSKV 960 Nicotiana Alata Nicotiana 47 RECKTESNTFPGICITKPPCRKACISEKFTDGHCSKI Plant Defensin tabacum LRRCLCTKPC 1 (Nad1) 961 osmotin Nicotiana 250 MSNNMGNLRSSFVFFLLALVTYTYAATIEVRNNCPY precursor tabacum TVWAASTPIGGGRRLDRGQTWVINAPRGTKMARV WGRTNCNFNAAGRGTCQTGDCGGVLQCTGWGKP PNTLAEYALDQFSGLDFWDISLVDGFNIPMTFAPTN PSGGKCHAIHCTANINGECPRELRVPGGCNNPCTT FGGQQYCCTQGPCGPTFFSKFFKQRCPDAYSYPQ DDPTSTFTCPGGSTNYRVIFCPNGQAHPNFPLEMP GSDEVAK 962 Osmotin-like Nicotiana 251 MSHLTTFLVFFLLAFVTYTYASGVFEVHNNCPYTVW protein tabacum AAATPVGGGRRLERGQSWWFWAPPGTKMARIWG precursor RTNCNFDGAGRGWCQTGDCGGVLECKGWGKPPN (Pathogenesis- TLAEYALNQFSNLDFWDISVIDGFNIPMSFGPTKPG related protein PGKCHGIQCTANINGECPGSLRVPGGCNNPCTTFG PR-5D) GQQYCCTQGPCGPTELSRWFKQRCPDAYSYPQD DPTSTFTCTSWTTDYKVMFCPYGSAHNETTNFPLE MPTSTHEVAK 963 Osmotin-like Lycopersicon 238 FFFLLAFVTYTYAATFEVRNNCPYTVWAASTPIGGG protein TPM-1 esculentum RRLDRGQTWVINAPRGTKMARIWGRTNCNFDGDG precursor (PR RGSCQTGDCGGVLQCTGWGKPPNTLAEYALDQFS P23) NLDFWDISLVDGFNIPMTFAPTNPSGGKCHAIHCTA (Fragment) NINGECPGSLRVPGGCNNPCTTFGGQQYCCTQGP CGPTDLSRFFKQRCPDAYSYPQDDPTSTFTCPSGS TNYRVVFCPNGVTSPNFPLEMPSSDEEAK 964 pathogenesis- Lycopersicon 233 AFVTYTYAATFEVRNNCPYTVWAASTPIGGGRRLD related protein esculentum RGQTWVINAPRGTKMARIWGRTNCNFDGAGRGSC P23 precursor QTGDCGGVLQCTGWGKPPNTLAEYALDQFSNLDF WDISLVDGFNIPMTFAPTNPSGGKCHAIHCTANING ECPGSLRVPGGCNNPCTTFGGQQYCCTQGPCGPT DLSRFFKQRCPDAYSYPQDDPTSTFTCPSGSTNYR VVFCPNGVTSPNFPLEMPSSDEEAK 965 plant defensin Arabidopsis 76 MKVSPRLNSALLLLFMILATVMGLVTVEARTCETSS protein, putative thaliana NLFNGPCLSSSNCANVCHNEGFSDGDCRGFRRRC (PDF2.4) LCTRPC 966 plant defensin- Arabidopsis 122 MERIPSLASLVSLLIIFATVVNQTRASICNDRLGLCDG fusion protein, thaliana CDQRCKAKHGPSCESKCDGPVGMLLCTCTYECGP putative TKLCNGGLGNCGESCNEQCCDRNCAQRYNGGHG YCNTLDDFSLCLCKYPC 967 Plant defensin- Pyrus 81 LVSTAFVLVLLLATIEMGPMGVEARTESSKAVEGKIC like protein pyrifolia EVPSTLFKGLCFSSNNCKHTCRKEQFTRGHCSVLT (Fragment) RACVCTKKC 968 probable Arabidopsis 80 MAKFCTTITLILVALVLFADFEAPTIVKAELCKRESET antifungal thaliana WSGRCVNDYQCRDHCINNDRGNDGYCAGGYPWY protein RSCFCFFSC [imported] 969 Probable Arabidopsis 80 MAKSAAIITFLFAALVLFAAFEAPIMVEAQKLCEKPS cysteine-rich thaliana GTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPA antifungal HKCICYFPC protein At2g26010 precursor (AFP) 970 Probable Arabidopsis 80 MAKFASIITFIYAALVLFAAFEVPTMVEAQKLCEKPS cysteine-rich thaliana GTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPA antifungal HKCICYVPC protein At2g26020 precursor (AFP) 971 Probable Arabidopsis 80 MAKFASIITLIFAALVLFAAFDAPAMVEAQKLCEKPS cysteine-rich thaliana GTWSGVCGNSNACKNQCINLEGAKHGSCNYVFPA antifungal HKCICYVPC protein LCR77 precursor (AFP) 972 Protease Pyrus 87 MEPSMRLISAAFVLILLLATTEMGPMGVEAKSKSSK inhibitor-like pyrifolia EVEKRTCEAASGKFKGMCFSSNNCANTCAREKFD protein GGKCKGFRRRCMCTKKC 973 Protease Pyrus 87 MERSMRLVSAAFVLVLLLAATEMGPMGVEARTESS inhibitor-like pyrifolia KAVEGKICEVPSTLFKGLCFSSNNCKHTCRKEQFTR protein GHCSVLTRACVCTKKC 974 Proteinase Capsicum 78 MAHSMRFFAIVLLLAMLVMATEMGPMRIVEARTCES inhibitor annuum QSHRFKGVCASETNCASVCQTEGFSGGDCRGFRR precursor RCFCTRPC 975 Putative Arabidopsis 78 MASSYTLMLFLCLSIFLIASTEMMAVEGRICERRSKT defensin AMP1 thaliana WTGFCGNTRGCDSQCKRWERASHGACHAQFPGF protein ACFCYFNC 976 Putative plant Picea abies 83 MADKGVGSRLSALFLLVLLVISIGMMQLEPAEGRTC defensin SPI1B KTPSGKFKGVCASRNNCKNVCQTEGFPSGSCDFH VANRKCYCSKPCP 977 sormatin Sorghum 22 AVFTVVNRCPYTVWAASVPVGG bicolor 978 TOM P14A Lycopersicon 41 AVHNDARAQVGVGPMSXDANLASRAQNYANSRAX protein esculentum DXNLIXS (Fragment) 979 TOM P14B Lycopersicon 35 DXLAVHNDARAQVGAGPMDANLASRAQNXANSRAG pathogenesis- esculentum related PR-1 protein (Fragments) 980 TOM P14C Lycopersicon 97 DYLNAHNAARRQVGVGPMTXDNRLAAFAQNYANQ pathogenesis- esculentum RADXRMQHSGGPYGENLAAAFPQLNCQAGKVCGH related PR-1 YTQVVWRNSVRLGCARVRCNNGWYFITCN protein (Fragments) 981 trimatin Triticum 23 ATITVVNRCSYTVWPGALPGGGA aestivum 982 Vicilin Macadamia 666 MAINTSNLCSLLFLLSLFLLSTTVSLAESEFDRQEYE integrifolia ECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSK YDNQDDPQTDCQQCQRRCRQQESGPRQQQYCQ RRCKEICEEEEEYNRQRDPQQQYEQCQERCQRHE TEPRHMQTCQQRCERRYEKEKRKQQKRYEEQQR EDEEKYEERMKEEDNKRDPQQREYEDCRRRCEQQ EPRQQYQCQRRCREQQRQHGRGGDLINPQRGGS GRYEEGEEKQSDNPYYFDERSLSTRFRTEEGHISV LENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLD ADAILLVTGGRGALKMIHRDNRESYNLECGDVIRIPA GTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAG GQNPEPYLSTFSKEILEAALNTQAERLRGVLGQQRE GVIISASQEQIRELTRDDSESRRWHIRRGGESSRGP YNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDVSV FIANITQGSMMGPFFNTRSTKVVVVASGEADVEMA CPHLSGRHGGRRGGKRHEEEEDVHYEQVKARLSK REAIVVPVGHPVVFVSSGNENLLLFAFGINAQNNHE NFLAGRERNVLQQIEPQAMELAFAAPRKEVEELFNS QDESIFFPGPRQHQQQSSRSTKQQQPLVSILDFVGF 983 Vicilin Macadamia 666 MAINTSNLCSLLFLLSLFLLSTTVSLAESEFDRQEYE integrifolia ECKRQCMQLETSGQMRRCVSQCDKRFEEDIDWSK YDNQEDPQTECQQCQRRCRQQESGPRQQQYCQR RCKEICEEEEEYNRQRDPQQQYEQCQKHCQRRET EPRHMQTCQQRCERRYEKEKRKQQKRYEEQQRE DEEKYEERMKEEDNKRDPQQREYEDCRRRCEQQE PRQQHQCQLRCREQQRQHGRGGDMMNPQRGGS GRYEEGEEEQSDNPYYFDERSLSTRFRTEEGHISV LENFYGRSKLLRALKNYRLVLLEANPNAFVLPTHLD ADAILLVIGGRGALKMIHHDNRESYNLECGDVIRIPA GTTFYLINRDNNERLHIAKFLQTISTPGQYKEFFPAG GQNPEPYLSTFSKEILEAALNTQTEKLRGVFGQQRE GVIIRASQEQIRELTRDDSESRHWHIRRGGESSRGP YNLFNKRPLYSNKYGQAYEVKPEDYRQLQDMDLSV FIANVTQGSMMGPFFNTRSTKVVVVASGEADVEMA CPHLSGRHGGRGGGKRHEEEEDVHYEQVRARLSK REAIVVLAGHPWFVSSGNENLLLFAFGINAQNNHE NFLAGRERNVLQQIEPQAMELAFAAPRKEVEESFN SQDQSIFFPGPRQHQQQSPRSTKQQQPLVSILDFV GF 984 Vicilin Macadamia 625 QCMQLETSGQMRRCVSQCDKRFEEDIDWSKYDNQ (Fragment) integrifolia EDPQTECQQCQRRCRQQESDPRQQQYCQRRCKE ICEEEEEYNRQRDPQQQYEQCQKRCQRRETEPRH MQICQQRCERRYEKEKRKQQKRYEEQQREDEEKY EERMKEGDNKRDPQQREYEDCRRHCEQQEPRLQ YQCQRRCQEQQRQHGRGGDLMNPQRGGSGRYE EGEEKQSDNPYYFDERSLSTRFRTEEGHISVLENFY GRSKLLRALKNYRLVLLEANPNAFVLPTHLDADAILL VIGGRGALKMIHRDNRESYNLECGDVIRIPAGTTFYL INRDNNERLHIAKFLQTISTPGQYKEFFPAGGQNPE PYLSTFSKEILEAALNTQTERLRGVLGQQREGVIIRA SQEQIRELTRDDSESRRWHIRRGGESSRGPYNLFN KRPLYSNKYGQAYEVKPEDYRQLQDMDVSVFIANIT QGSMMGPFFNTRSTKVVVVASGEADVEMACPHLS GRHGGRGGGKRHEEEEEVHYEQVRARLSKREAIV VLAGHPVVFVSSGNENLLLFAFGINAQNNHENFLAG RERNVLQQIEPQAMELAFAASRKEVEELFNSQDESI FFPGPRQHQQQSPRSTKQQQPLVSILDFVGF 985 Wheatwin1 Triticum 146 MAARPMLVVALLCAAAAAATAQQATNVRATYHYYR precursor aestivum PAQNNWDLGAPAVSAYCATWDASKPLSWRSKYG (Pathogenesis- WTAFCGPAGAHGQASCGKCLQVTNPATGAQITARI related protein VDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLNVN 4a) (Protein YQFVDCRD 0.14) 986 Wheatwin2 Triticum 148 MTMAARLMLVAALLCAAAAAATAQQATNVRATYHY precursor aestivum YRPAQNNWDLGAPAVSAYCATWDASKPLSWRSKY (Pathogenesis- GWTAFCGPAGAHGQAACGKCLRVTNPATGAQITA related protein RIVDQCANGGLDLDWDTVFTKIDTNGIGYQQGHLN 4b) VNYQFVDCRD 987 Zeamatin Zea mays 206 AVFTVVNQCPFTVWAASVPVGGGRQLNRGESWRI TAPAGTTAARIWARTGCKFDASGRGSCRTGDCGG VLQCTGYGRAPNTLAEYALKQFNNLDFFDISLIDGF NVPMSFLPDGGSGCSRGPRCAVDVNARCPAELRQ DGVCNNACPVFKKDEYCCVGSAANDCHPTNYSRY FKGQCPDAYSYPKDDATSTFTCPAGTNYKVVFCP 988 Zeamatin Zea mays 227 MAGSVAIVGIFVALLAVAGEAAVFTVVNQCPFTVWA precursor ASVPVGGGRQLNRGESWRITAPAGTTAARIWARTG CKFDASGRGSCRTGDCGGVLQCTGYGRAPNTLAE YALKQFNNLDFFDISLIDGFNVPMSFLPDGGSGCSR GPRCAVDVNARCPAELRQDGVCNNACPVFKKDEY CCVGSAANDCHPTNYSRYFKGQCPDAYSYPKDDA TSTFTCPAGTNYKVVFCP

TABLE 2 Defensins SEQ ID NO: Name Organism Sequence 989 HNP-1 Human A C Y CR IPA C IAG ER RY G T C IYQ G RLWAF CC 990 HNP-2 Human C Y CR IPA C IAG ER RY G T C IYQ G RLWAF CC 991 HNP-3 Human D C Y CR IPA C IAG ER RY G T C IYQ G RLWAF CC 992 HNP-4 Human V C S CR LVF C RRT E L R V G N C LI G GVSFTY CC TRV 993 NP-1 Rabbit VV C A CR RAL C LPR ER RA G F C RIR G RIHPL CC RR 994 NP-2 Rabbit VV C A CR RAL C LPL ER RA G F C RIR G RIHPL CC RR 995 NP-3A Rabbit GI C A CR RRF C PNS ER FS G Y C RVN G ARYVR CC SRR 996 NP-3B Rabbit GR C V CR KQLL C SYR ER RI G D C KIR G VRFPF CC PR 997 NP-4 Rabbit VS C T CR RFS C GFG ER AS G S C TVN G VRHTL CC RR 998 NP-5 Rabbit VF C T CR GFL C GSG ER AS G S C TIN G VRHTL CC RR 999 RatNP-1 Rat VT C Y CR RTR C GFR ER LS G A C GYR G RIYRL CC R 1000 Rat-NP-3 Rat C S CR YSS C RFG ER LLS G A C RLN G RIYRL CC 1001 Rat-NP-4 Rat A C T CR IGA C VSG ER LT G A C GLN G RIYRL CC R 1002 GPNP Guinea pig RR C I C TTRT C RFPY R RL G T C IFQNRVYTF C C

B. Growth Factors

In some embodiments of the present invention, trophic factor combinations for treating injured nervous systems comprise one or more growth factors. Growth factors useful in the present invention include, but are not limited to, the following broad classes of cytoactive compounds: Insulin, Insulin like growth factors such as IGF-I, IGF-IB, IGF-II, and IGF-BP; Heparin-binding growth factors such as Pleiotrophin (NEGF1) and Midkine (NEGF2); PC-cell derived growth factors (PCDGF); Epidermal Growth Factors such as α-EGF and β-EGF; EGF-like molecules such as Keratinocyte-derived growth factor (which is identical to KAF, KDGF, and amphiregulin) and vaccinia virus growth factor (VVGF); Fibroblast Growth Factors such as FGF-1 (Basic FGF Protein), FGF-2 (Acidic FGF Protein), FGF-3 (Int-2), FGF-4 (Hst-1), FGF-5, FGF-6, and FGF-7 (identical to KGF); FGF-Related Growth Factors such as Endothelial Cell Growth Factors (e.g., ECGF-α and ECGF-β); FGF- and ECGF-Related Growth Factors such as Endothelial cell stimulating angiogenesis factor and Tumor angiogenesis factor, Retina-Derived Growth Factor (RDGF), Vascular endothelium growth factors (VEGF, VEGF-B, VEGF-C, and VEGF-D), Brain-Derived Growth Factor (BDGF A- and -B), Astroglial Growth Factors (AGF 1 and 2), Omentum-derived factor (ODF), Fibroblast-Stimulating factor (FSF), and Embryonal Carcinoma-Derived Growth Factor; Neurotrophic Growth Factors such as α-NGF, β-NGF, γ-NGF, Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF); Glial Growth Factors such as GGF-I, GGF-II, GGF-III, Glia Maturation Factor (GMF), and Glial-Derived Nuerotrophic Factor (GDNF); Organ-Specific Growth Factors such as Liver Growth Factors (e.g., Hepatopoietin A, Hepatopoietin B, and Hepatocyte Growth Factors (HCGF or HGF), Prostate Growth Factors (e.g., Prostate-Derived Growth Factors [PGF] and Bone Marrow-Derived Prostate Growth Factor), Mammary Growth Factors (e.g., Mammary-Derived Growth Factor 1 [MDGF-1] and Mammary Tumor-Derived Factor [MTGF]), and Heart Growth Factors (e.g., Nonmyocyte-Derived Growth Factor [NMDGF]); Cell-Specific Growth Factors such as Melanocyte Growth Factors (e.g., Melanocyte-Stimulating Hormone [α-, β-, and γ-MSH] and Melanoma Growth-Stimulating Activity [MGSA]), Angiogenic Factors (e.g., Angiogenin, Angiotropin, Platelet-Derived ECGF, VEGF, and Pleiotrophin), Transforming Growth Factors (e.g., TGF-α, TGF-β, and TGF-like Growth Factors such as TGF-β₂, TGF-β₃, TGF-e, GDF-1, GDF-9, CDGF and Tumor-Derived TGF-β-like Factors), ND-TGF, and Human epithelial transforming factor [h-TGFe]); Regulatory Peptides with Growth Factor-like Properties such as Bombesin and Bombesin-like peptides (e.g., Ranatensin, and Litorin], Angiotensin, Endothelin, Atrial Natriuretic Factor, Vasoactive Intestinal Peptide, and Bradykinin; Cytokines such as connective tissue growth factor (CTGF), the interleukins IL-1 (e.g., Osteoclast-activating factor (OAF), Lymphocyte-activating factor (LAF), Hepatocyte-stimulating factor (HSF), Fibroblast-activating factor (FAF), B-cell-activating factor (BAF), Tumor inhibitory factor 2 (TIF-2), Keratinocyte-derived T-cell growth factor (KD-TCGF)), IL-2 (T-cell growth factor (TCGF), T-cell mitogenic factor (TCMF)), IL-3 (e.g., Hematopoietin, Multipotential colony-stimulating factor (multi-CSF), Multilineage colony-stimulating activity (multi-CSA), Mast cell growth factor (MCGF), Erythroid burst-promoting activity (BPA-E), IL-4 (e.g., B-cell growth factor I (BCGF-I), B-cell stimulatory factor 1 (BSF-1)), IL-5 (e.g., B-cell growth factor II (BCGF-II), Eosinophil colony-stimulating factor (Eo-CSF), Immunoglobulin A-enhancing factor (IgA-EF), T-cell replacing factor (TCRF)), IL-6 (B-cell stimulatory factor 2 (BSF-2), B-cell hybridoma growth factor (BCHGF), Interferon β₂ (IFN-B), T-cell activating factor (TAF), IL-7 (e.g., Lymphopoietin 1 (LP-1), Pre-B-cell growth factor (pre-BCGF)), IL-8 (Monocyte-derived neutrophil chemotactic factor (MDNCF), Granulocyte chemotatic factor (GCF), Neutrophil-activating peptide 1 (NAP-1), Leukocyte adhesion inhibitor (LAI), T-lymphocyte chemotactic factor (TLCF)), IL-9 (e.g., T-cell growth factor III (TCGF-III), Factor P40, MegaKaryoblast growth factor (MKBGF), Mast cell growth enhancing activity (MEA or MCGEA)), IL-10 (e.g., Cytokine synthesis inhibitory factor (CSIF)), IL-11 (e.g., Stromal cell-derived cytokine (SCDC)), IL-12 (e.g., Natural killer cell stimulating factor (NKCSF or NKSF), Cytotoxic lymphocyte maturation factor (CLMF)), TNF-α (Cachectin), TNF-β (Lymphotoxin), LIF (Differentiation-inducing factor (DIF), Differentiation-inducing activity (DIA), D factor, Human interleukin for DA cells (HILDA), Hepatocyte stimulating factor III (HSF-III), Cholinergic neuronal differentiation factor (CNDF), CSF-1 (Macrophage colony-stimulating factor (M-CSF)), CSF-2 (Granulocyte-macrophage colony-stimulating factor (GM-CSF)), CSF-3 (Granulocyte colony-stimulating factor (G-CSF)), and erythropoietin; Platelet-derived growth factors (e.g., Placental growth factor (PlGF), PDGF-A, PDGF-B, PDGF-AB, p28-sis, and p26-cis), and Bone Morphogenetic proteins (e.g., BMP and BMP-15), neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y), and neurotransmitters (e.g., norepinephrine and acetylcholine).

Suitable growth factors may be obtained from commercial sources, purified from natural sources, or be produced by recombinant methods. Recombinant growth factors can be produced from wild-type coding sequences or from variant sequences that encode functional growth factors. Suitable growth factors also include analogs that may be smaller peptides or other molecules having similar binding and biological activity as the natural growth factors. Methods for producing growth factors are described in U.S. Pat. Nos. 5,183,805; 5,218,093; 5,130,298; 5,639,664; 5,457,034; 5,210,185; 5,470,828; 5,650,496; 5,998,376; and 5,410,019; all of which are incorporated herein by reference.

C. Neurotrophins

The trophic factor combinations provided herein also can include one or more neurotrophic growth factors such as Brain-Derived Neurotrophic Factor (BDNF), Neurotrophin-3, Neurotrophin-4, and Ciliary Nuerotrophic Factor (CNTF).

Nerve growth factors, such as α-NGF, β-NGF, γ-NGF, and the like, are neurotrophins. In an embodiment, the trophic factor combination does not include a nerve growth factor, which results in lessened pain.

D. Neuropeptides

The trophic factor combinations provided herein also can include one or more neuropeptides, e.g., PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide (MAB-alpha-NP); Beta-SG neuropeptide (MAB-beta-NP)); Pheromone biosynthesis activating neuropeptide (M); PBAN-type neuropeptides (e.g., Diapause hormone (DH); Alpha-SG neuropeptide (Alpha-SGNP); Beta-SG neuropeptide (Beta-SGNP); Pheromone biosynthesis activating neuropeptide I (PBAN-I) (BoM)); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7) (Fragment); neuropeptides [similarity]; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)); Pol-RFamide neuropeptides; Antho-RFamide neuropeptides type 1; LWamide neuropeptides (e.g., LWamide I; Metamorphosin A (LWamide II) (MMA); LWamide III; LWamide IV; LWamide V; LWamide VI; LWamide VII; LWamide VIII; LWamide IX); Antho-RFamide neuropeptides type 2; Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide-27 (PACAP-27) (P)); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWS); Glucagon-family neuropeptides (e.g., Growth hormone-releasing factor (GRF) (Growth hormone-releasing hormone) (GHRH); Pituitary adenylate cyclase activating polypeptide (PACAP)]; FMRFamide-like neuropeptides); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (AgI-PBAN); Gamma-SG neuropeptid; FMRFamide-related neuropeptides; Myomodulin neuropeptides (e.g., GLQMLRL-amide; QIPMLRL-amide; SMSMLRL-amide; SLSMLRL-amide; Myomodulin A (PMSMLRL-amide)); FMRFamide neuropeptides; neuropeptides (e.g., Substance P, calcitonin gene-regulated peptide, and neuropeptide Y); LWamide neuropeptides (e.g., LWamide I; LWamide II; LWamide III; LWamide IV; LWamide V; LWamide VI; Metamorphosin A (MMA); Mwamide) (Fragment); PBAN-type neuropeptides (e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide); Pheromone biosynthesis activating neuropeptide (HeA-PBAN); Gamma-SG neuropeptid; Antho-RFamide neuropeptides; Neuropeptides capa receptor (Cap2b receptor); Neuropeptides B/W receptor type 2 (G protein-coupled receptor 8); Neuropeptides B/W receptor type 1 (G protein-coupled receptor 7); FMRFamide-like neuropeptides [e.g., Neuropeptide AF10 (GFGDEMSMPGVLRF-amide); Neuropeptide AF20 (GMPGVLRF-amide); Neuropeptide AF3 (AVPGVLRF-amide); Neuropeptide AF4 (GDVPGVLRF-amide); N PBAN-type neuropeptides [e.g., Diapause hormone homolog (DH); Alpha-SG neuropeptide; Beta-SG neuropeptide; Pheromone biosynthesis activating neuropeptide (HeZ-PBAN); Gamma-SG neuropeptid; FMRFamide neuropeptides type FMRF-1 (Fragment); Abdominal ganglion neuropeptides L5-67 (e.g., Luqin; Luqin-B; Luqin-C; Proline-rich mature peptide (PRMP)); FMRFamide neuropeptides type FMRF-2; FMRFamide neuropeptides type FMRF-4 (Fragment); Myomodulin neuropeptides (e.g., Myomodulin A (MM-A) (PMSMLRL-amide) (Neuron B16 peptide); Myomodulin B (MM-B) (GSYRMMRL-amide); Myomodulin D (MM-D) (GLSMLRL-amide); Myomodulin F (MM-F); LWamide neuropeptides (e.g., LWamide I; LWamide II; Metamorphosin A (MMA); Iwamide) (Fragment) (Substance P, calcitonin gene-regulated peptide, and neuropeptide Y.)

E. Other Components

The trophic factor combinations can be used with various delivery systems. In some embodiments, the trophic factor combination is mixed with a viscous substance to increase the viscosity of the combination. The increased viscosity retains the trophic factor combination at the site of the injury longer than it would be retained in the absence of the viscous substance. The viscous substance can be, for example, a polysaccharide, such as hyaluranic acid.

In another embodiment, the trophic factor combination is delivered in a slow release formula, such as in a matrix, for example, a woundhealing matrix, either with or without a viscous substance. In an embodiment, the matrix is a hydrogel, such as a hydrogel disclosed in U.S. Patent Application No. US 20030083389A1, which describes hydrogels wherein a polymer matrix is modified to contain a bifunctional poly(alkylene glycol) molecule covalently bonded to the polymer matrix. The hydrogels can be cross-linked using, for example, glutaraldehyde. The hydrogels can also be crosslinked via an interpenetrating network of a photopolymerizable acrylates. In one embodiment of the invention, the components of the trophic factor combination are incorporated into the hydrogel, for example, through covalent bonds to poly(alkylene glycol) molecules of the hydrogel or through entertainment within the hydrogel. In other embodiments, the matrix is a collagen gel matrix, which can be impregnated with a trophic factor combination. Other matrices can also be used.

The trophic factor combination can also be delivered in a base solution, such as UW solution (DuPont Critical Care, Waukegan, Ill.), or other base solutions.

The neurochemical combinations can be used in conjunction with cell therapy, where transfected cells are produced to release the ingredients and obtain continual delivery of a trophic factor combination. For example, embryonic or adult stem cells can be modified to express trophic factors, antimicrobial peptides, and other relevant neurochemicals, to deliver the trophic factor combination endogenously to the injured spinal cord. In the case of genetically modified cell transplants, the transfected cells can be tagged with cell surface antigens so that the cells can be controlled. For example, antibodies targeting the specific antigen could be used to kill the implanted cells after therapeutic results have been achieved.

Delivery of the neurochemical combinations can also be achieved by media with spaced supports, such as sponges, gels, or biopolymers.

F. Exemplary Formulations

A trophic factor combination includes one or more antimicrobial peptide and/or one or more substance having an antimicrobial peptide effect, alone or with one or more of the following trophic factors: growth factors, neuropeptides, and neurotrophins. Another trophic factor combination includes a viscous substance, such as hyaluronic acid, among others. Another trophic factor combination includes other cytoactive compounds, such as one or more cytokine and/or one or more chemokine. Non-limiting examples of these trophic factor combinations are provided in Tables 3a-3h below. It will be recognized that the trophic factor combinations can comprise one or more antimicrobial polypeptides (e.g., a defensin such as BNP-1). The trophic factor combinations described below can also comprise one or more trophic factors above. Accordingly, in some preferred embodiments, the trophic factor combination is supplemented with one or more of the following trophic factors: trehalose (Sigma, St. Louis Mo.; e.g., about 15 mM), substance P (Sigma; e.g., about 10 μg/ml), IGF-1 (Collaborative Biologicals; e.g., about 10 ng/ml), EGF (Sigma; e.g., about 10 ng/ml), and BDNF (2 μg/ml). In some preferred embodiments, the trophic factor combination is also supplemented with insulin (1-200 units, preferably 40 units) prior to use. In some embodiments, an antimicrobial polypeptide is not included in the trophic factor combination.

In some exemplary embodiments, EGF and/or IGF-1 are included in the trophic factor combination at a concentration of about 1 ng/ml to about 100 ng/ml, most preferably about 10 ng/ml. In other exemplary embodiments, substance P is included at a concentration of about 0.1 μg/ml to about 100 μg/ml, most preferably about 2.5 μg/ml.

It will be recognized that the Tables below provide formulations that are exemplary and non-limiting. For example, alterations in the specific substances used and the number of those substances are all within the scope of the invention. In some embodiments, the antimicrobial polypeptide and/or substance having an antimicrobial peptide effect and/or one or more trophic factor, are provided in stable form that can be reconstituted. Methods for stabilization include, for example, lyophilization. In embodiments where the antimicrobial polypeptide and/or one or more growth factors are provided in lyophilized form, they can conveniently reconstituted prior to use, for example, in sterile water or in an aliquot of a base medium (e.g., UW solution), prior to addition to a base medium (e.g., hyaluronic acid, UW solution).

Alternatively, the at least one microbial polypeptide and/or one or more trophic factor can be provided as a separate composition (i.e., a “bullet”) that is added to a base medium. In preferred embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more trophic factor as described above. In some embodiments, the bullet contains an antimicrobial peptide and/or a substance having an antimicrobial peptide effect and/or one or more of the trophic factor as described above in concentrations that provide the appropriate concentration when added to a specific volume of the base medium, where used.

TABLE 3a Component Type Substance Antimicrobial peptide BNP-1

TABLE 3b Component Type Substance Antimicrobial peptide BNP-1 Growth factor IGF-1

TABLE 3c Component Type Substance Antimicrobial peptide BNP-1 Neuropeptide Substance P

TABLE 3d Component Type Substance Antimicrobial peptide BNP-1 Neurotrophin BDNF

TABLE 3e Component Type Substance Antimicrobial peptide BNP-1 Growth factor IGF-1 Neuropeptide Substance P

TABLE 3f Component Type Substance Antimicrobial peptide BNP-1 Growth factor IGF-1 Neurotrophin BDNF

TABLE 3g Component Type Substance Antimicrobial peptide BNP-1 Neuropeptide Substance P Neurotrophin BDNF

TABLE 3h Component Type Substance Antimicrobial peptide BNP-1 Growth factor IGF-1 Neuropeptide Substance P Neurotrophin BDNF

It is contemplated that the trophic factor combination can be provided in a pre-formulated form, such as in a kit format. The kit can include (1) at least one of an antimicrobial peptide and a substance having an antimicrobial peptide effect and (2) a neurotrophin. The kit can also include a viscous substance. At least one of a growth factor and a neuropeptide can also be included.

II. Uses of Trophic Factor Combinations and Their Individual Components

It is contemplated that the trophic factor combinations and their individual components described above may be utilized in a variety of procedures related to injury to the nervous system and other medical procedures. It is contemplated that the trophic factor combinations and their individual components can be used for the treatment of any part of the nervous system, including the central nervous system and the peripheral nervous system.

In one embodiment, the trophic factor combinations or one or more of their individual components are used during surgery of the disc and/or other portions of the nervous system. In an embodiment, a trophic factor combination or one or more of their individual components applied to surgical hardware and/or other implants, such as surgical screws, plates, pins, clamps, wires, pins, rods, nails, probes, spinal fixation devices, and the like. In another embodiment, a trophic factor combination or one or more of their individual components is applied directly during surgery, such as to a surgical opening, for example, an incision, a section, or any other opening. In one embodiment, a trophic factor combination or one or more of their individual components is applied to one or more tissue, nerve, organ, or cavity. A trophic factor combination or one or more of their individual components can also be applied to a surgical instrument such that when the instrument is used, the trophic factor combination or one or more of their individual components is delivered to injury and/or surrounding tissue, fluid, organ, and the like.

In use, an injury to the nervous system is identified. At least one component of the trophic factor combination is applied to the injury to the nervous system.

In some embodiments, the trophic factor combinations can be utilized to reduce body weight loss post injury in injured animals treated with the combination when compared to injured animals not treated with the trophic factor combination. Preferably, the decrease in loss of body weight is improved by at least 25% and more preferably by at least 50% as compared to animals not receiving the trophic factor combination. In some embodiments, the trophic factor combinations are used to strengthen motor recovery in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to increase evoked potential amplitudes in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. In some embodiments, the trophic factor combinations are used to lower the current required to evoke a response (threshold current) in injured animals treated with the trophic factor combination when compared to injured animals not treated with the trophic factor combination. Application of the trophic factor combination according to the invention can also have at least one of the following additional effects: reduced pain in the animal, a neuroprotective effect, triggered neuronal plasticity, reduced inflammation, and growth of new cells.

EXAMPLES

The following examples serve to illustrate certain preferred embodiments and aspects of the present invention and are not to be construed as limiting the scope thereof.

Example 1 Materials and Methods

Experiments were performed on 3-5 month old male Sprague-Dawley (SD) and Lewis rats that were housed individually with free access to food and water. Rats were placed into four groups: 1) spinally injured SD rats without a trophic factor combination administered (n=8), 2) spinally injured SD rats with a trophic factor combination (n=2); 3) spinally injured Lewis rats without a trophic factor combination administered (n=5), and 4) spinally injured Lewis rats with a trophic factor combination administered (n=2).

Spinal cord injury. Rats were anesthetized with medetomidine (75 μg/kg i.m.) and isoflurane in oxygen. After oro-tracheal intubation, anesthesia was maintained with isoflurane in oxygen and rats were mechanically ventilated. A laminectomy was made at the second cervical vertebral level to allow the second cervical spinal segment and the cranial segment of the third cervical spinal segment to be exposed. A 1-mm-long left-sided hemisection was made in the cranial segment of C₂ and the section aspirated with a fine tipped glass pipette. The surgical wound was closed using standard techniques. All animals were allowed to recover and received atipamezole (0.1 mg/kg i.v.) to antagonize the anesthetic effects of medetomidine. Buprenorphine (50 μg/kg i.v.) and carprofen (5 mg/kg i.v.) were administered for postsurgical pain control. Analgesics were repeated as required over the next 2 days.

Trophic Factor Combination. The trophic factor combination (also referred to as the trophic factor combination) was made by adding 10 ug of BNP-1 (bactenecin), 100 ng of insulin-like growth factor (IGF-1), and 25 mg of Substance P to 200 ul of distilled water.

Trophic factor combination administration. Prior to closure of the surgical wound, hyaluronic acid (Hylartin V, sodium hyalurate) (10%) was added to the neurotrophin mixture to thicken the solution and improve retention at the site of spinal injury. Two ug of BDNF was added to 0.4-0.45 ml of the mixture. The mixture (0.4-0.45 ml) was then administered using a syringe and 22-gauge needle into the hemisection cavity. The wound was closed immediately after injection.

Experimental preparation. Two weeks after surgical spinal injury, respiratory motor output was measured from both phrenic nerves using two distinct experimental techniques. First, spontaneous (brain-stem driven) phrenic motor activity was measured in anesthetized rats during standardized conditions. Second, spontaneous activity was removed by hyperventilating the rats and evoke potentials were elicited by spinal stimulation to evaluate the strength of the spinal pathways contributing to motor recovery.

Isoflurane anesthesia was induced in a closed chamber and maintained (2.5-3.5%) via nose cone while rats were tracheotomized. Rats were mechanically ventilated following tracheal cannulation. Following femoral venous catheterization rats were converted to urethane anesthesia (1.6 g/kg) then bilaterally vagotomized and paralyzed with pancuronium bromide (2.5 mg/kg, i.v.). Blood pressure was monitored via a femoral arterial catheter and pressure transducer (Gould P23ID, Valley View, Ohio). End-tidal CO₂ was monitored with a rapidly responding analyzer (Novametrix, Wallingford, Conn.). Arterial partial pressures of O₂ (PaO₂) and CO₂ (PaCO₂) as well as pH were determined from 0.2 ml blood samples (ABL-500, Radiometer, Copenhagen, Denmark); unused blood was returned to the animal. Rectal temperature was maintained (37-39° C.) with a heated table. Phrenic nerves were isolated with a dorsal approach, cut distally, desheathed, bathed in mineral oil and placed on bipolar silver electrodes. Nerve activity was amplified (1000-10,000×) and filtered (100-10,000 Hz bandpass; model 1800, A-M Systems, Carlsborg, Wash.).

Spontaneous phrenic motor output. In all rats, the CO₂ apneic threshold for inspiratory activity in the phrenic nerve contralateral to hemisection was determined after waiting a minimum of one hour following conversion to urethane anesthesia. This delay allowed blood pressure and respiratory motor output to stabilize. The procedure to establish the apneic threshold began by increasing the ventilator frequency until inspiratory activity ceased. Ventilator rate was then decreased slowly until inspiratory activity re-appeared. The end-tidal CO₂ partial pressure (P_(ET)CO₂) corresponding to the onset of inspiratory bursting was defined as the CO₂ apneic threshold. P_(ET)CO₂ was maintained 3 mmHg above the apneic threshold by adjusting the ventilator pump rate and inspired CO₂ content. After the CO₂ apneic threshold and baseline PaCO₂ levels were established, 30-45 minutes were allowed to attain stable baseline conditions.

Evoked phrenic potentials. Rats were hyperventilated (PaCO₂<30 mmhg) to prevent spontaneous inspiratory efforts. A monopolar tungsten electrode (5 MΩ, A-M Systems) was inserted contralateral to the spinal hemisection and adjacent to the C2 dorsal roots. The electrode tip was placed in or in close proximity to the ventrolateral finiculus (1.8-2.3 mm below the dorsal root entry zone). Electrode position was selected by maximizing the amplitude of a short latency (<1.0 ms) evoked potential in the phrenic nerve contralateral to SCI. Stimulus-response relationships were obtained by applying current pulses (20-1000 μA, 0.2 ms duration) with a stimulator (model S88, Grass Instruments, Quincy, Mass.) and stimulus isolation unit (model PSIU6E, Grass Instruments). Phrenic potentials were digitized and analyzed with P-CLAMP software (Axon Instruments, Foster City, Calif.).

Results:

Body Weight. Body weight decreased by 2 weeks post-injury in rats that had received a spinal hemisection (FIG. 1). Decreased body mass may represent disuse atrophy of skeletal muscles or inadequate caloric intake. Reduced food consumption may occur secondary to spinal cord injury because of motor paresis, reduced locomotor coordination, and/or decreased appetite. Spinally injured rats that received the trophic factor combination had significantly less reduction in body weight compared to the control group (FIG. 1).

Spontaneous Phrenic Nerve Activity. Spontaneous recovery of phrenic motor function on the injured side was evident as inspiratory bursts that were in synchrony with phrenic motor activity on the uninjured side. Phrenic motor recovery was present in all spinally injured rats regardless of treatment. However, the magnitude of this recovery differed between groups (FIG. 2). Administration of the trophic factor combination at the time of injury strengthened motor recovery at 2 weeks post-injury as evident by the significantly larger peak inspiratory voltage during baseline recording conditions (FIG. 2). Phrenic peak inspiratory voltage is correlated to tidal volume. Although tidal volume was not measured in these rats, it is reasonable to assume that the increased peak inspiratory voltage would translate to larger tidal volumes in these animals compared to spinally injured rats that did not receive the trophic factor combination.

Evoked Phrenic Nerve Potentials. Evoked potentials were recorded from the phrenic nerve on the side of injury (FIG. 3). Consistent with the effects of treatment on spontaneous phrenic nerve activity data, administration of trophic factor combination at the time of injury significantly increased evoked potential amplitudes compared to rats that only received a spinal injury.

In addition, a strong trend existed for the current required to evoke a response (threshold current) to be lower after trophic factor combination administration compared to the control group (FIG. 4). Collectively, these data suggest that the trophic factor combination strengthens motor recovery via a spinal mechanism that strengthens existing synaptic pathways onto phrenic motoneurons.

Example 2

This study was performed to determine whether application of a trophic factor combination can improve motor function after spinal cord injury (SCI). In this study, the trophic factor combination of Example 1 was applied and included insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P. The trophic factor combination was applied to test whether this combination would augment spontaneous respiratory motor recovery in a well-defined model of high cervical incomplete spinal cord injury (C2 hemisection). The trophic factor combination was applied to the injured spinal cord at the time of surgical injury. At 2 weeks post-injury, respiratory motor output was recorded bilaterally from phrenic nerves in urethane anesthetized, vagotomized, and mechanically ventilated spinally injured Lewis male rats (SCI-only: n=6; SCI+trophic factor combination; n=6, with some of these rats being the same as the rats in Example 1). Body weight decreased in all rats after injury. However, the change in body weight was significantly less after trophic factor combination treatment (see FIG. 5; p<0.05). Spontaneous recovery of phrenic motor output on the side of injury was present in all rats and represents activation of a latent population of bulbospinal premotor synaptic pathways to ipsilateral phrenic motoneurons that cross the spinal midline caudal to injury. The trophic factor combination increased the amplitude of phrenic inspiratory bursts on the injured side when measured as rectified and moving-averaged voltages and indexed to the maximal amplitude during hypercapnia (see FIG. 5; p<0.05). In contrast, the trophic factor combination did not alter phrenic motor output on the side opposite injury. Thus, combined treatment with the trophic factor combination improves phrenic motor recovery after C2 hemisection by selectively augmenting crossed spinal synaptic pathways.

Example 3

Subtractive studies. Experiments can be performed on rats in accordance with the methods described in Example 2 except that fewer than all four components, i.e., insulin-like growth factor (IGF-1), brain-derived neurotrophic factor (BDNF), bactenesin (BNP-1), and substance P, of the trophic factor combination can be used (except for one or more controls using all four components). Different components can also be used. For example, a different growth factor (and/or neurotrophin and/or neuropeptide and/or antimicrobial peptide) can be used than the one listed above. Studies can also be run using only one component, i.e., either IGF-1, BDNF, BNP-1, or substance P or any other trophic factor to determine the effects of the individual components. Studies can also be performed using combinations of two of the components and using combinations of three of the components to determine whether all four components are needed to achieve the desired results.

Example 4

Experiments can be performed on dogs having herniated discs. Traditionally, many dogs undergo surgical treatment of disc herniation, but no trophic factor combination has been administered during such surgery. Four naïve dogs can be first treated to test for unanticipated common severe negative effects of the trophic factor combination. Once this is done, 50 dogs presenting to the Veterinary Medical Teaching Hospital (VTMH) at the University of Wisconsin with severe spinal cord dysfunction can be tested.

Trophic factor combination. The trophic factor combination can be formulated of insulin like growth factor-1 (IGF-1) (10 ng/ml), substance P (2.5 μg/ml), bactenecin (1 μg/ml) and brain derived neurotrophic factor (BDNF) (2 μg/ml). The factors can be dissolved in a 1% hyaluronic acid solution. The hyaluronic acid is used in order to increase the contact time of the factors with the tissues.

Dogs that are clinical patients. Surgery can be performed under general anesthesia. A hemilaminectomy can be done at the site of the disc herniation. A 22-gauge catheter can be placed through the dura mater and arachnoid membrane and inserted in the subarachnoid space just caudal to the disc herniation. One ml of the trophic factor combination can be injected in the subarachnoid space. The surgery site can be closed routinely.

After recovery from anesthesia, intravenous lactated Ringer's solution and analgesics can be continued until the dog is able to drink on its own and does not appear painful. Neurologic examinations can be done twice a day. The dogs can be discharged to the owner when they are considered not to need pain medication, can urinate on their own, and are eating and drinking. Follow up examinations can be scheduled as appropriate clinically.

Pain or discomfort during surgery can be alleviated by maintenance of a surgical plane of anesthesia and constant rate infusion (CRI) of fentanyl 10 μg/kg/hr. The fentanyl CRI can be continued up to 12 hours post operatively at a dose of 2-5 μg/kg/hr. A Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours) can be administered as a routine postoperative treatment. Butorphanol can be further administered if the dogs demonstrate discomfort and can be given as long as clinical signs of pain, as indicated by abnormal posturing, vocalization, or discomfort upon palpation of the surgical wound site are present.

Immediately after surgery, the dogs can be monitored continuously until the animals are able to drink water on their own sufficient to maintain their hydration. After this recovery period, the animals can be checked a minimum of 3 times daily to determine if they are experiencing pain or discomfort. The dogs can be evaluated by physical exam, neurological exam, and direct palpation of the surgical wound. The dogs can receive routine recumbent care.

Dogs can be monitored post-surgically for cardiovascular stability by physical exam, pulse character, capillary refill time, heart rate, respiratory rate, and packed cell volume, if needed. Fluids can be administered if needed to maintain hydration. Postoperative discomfort can be alleviated by administration of fentanyl CRI (10 μg/kg/hr) during surgery and fentanyl CRI (2-5 μg/kg/hr) after surgery or butorphanol (0.2-0.4 mg/kg/IV or SQ) every 4-6 hours thereafter and a Fentanyl Patch (50 mcg/hr, 5 mcg/kg/hr for total of 72 hours).

Example 5

Safety trial of trophic factor combination on dogs. The toxicity of the trophic factor combination described in Example 4 was tested on dogs. Four beagle dogs were studied over a three-day period. While the dogs were anesthetized, the trophic factor combination described in Example 4 in hyaluronic acid was injected into 1) the lumbar cerebrospinal fluid (2 dogs) and 2) the cistema magna cerebrospinal fluid (2 dogs). In all four cases, the dogs recovered easily and showed no signs of toxic reactions. There was no evidence for chronic pain on neurological exam. All dogs were euthanized on the third day of the study. In summary, no adverse reactions were observed in any animal.

It is understood that the various preferred embodiments are shown and described above to illustrate different possible features of the invention and the varying ways in which these features may be combined. Apart from combining the different features of the above embodiments in varying ways, other modifications are also considered to be within the scope of the invention.

The invention is not intended to be limited to the preferred embodiments described above, but rather is intended to be limited only by the claims set out below. Thus, the invention encompasses all alternate embodiments that fall literally or equivalently within the scope of these claims. 

What is claimed is:
 1. A method of treating an injury to a nervous system of an animal, the method comprising: applying to the injury an effective amount of an antimicrobial peptide, BDNF, IGF-1, and Substance P, wherein the antimicrobial peptide is BNP-1 and wherein the injury comprises an acute spinal cord injury.
 2. The method of claim 1, wherein a viscous substance is applied with the BNP-1, BDNF, IGF-1, and Substance P.
 3. The method of claim 2, wherein the viscous substance comprises a polysaccharide.
 4. The method of claim 2, wherein the viscous substance comprises hyaluronic acid.
 5. The method of claim 1, wherein the BNP-1, BDNF, IGF-1, and Substance P are delivered in a slow release formula.
 6. The method of claim 5, wherein the slow release formula is a matrix.
 7. The method of claim 6, wherein the matrix includes a viscous substance.
 8. The method of claim 6, wherein the matrix is a hydrogel.
 9. The method of claim 8, wherein the hydrogel is a polymer matrix modified to contain a bifunctional poly(alkylene glycol) molecule covalently bonded to the polymer matrix.
 10. The method of claim 8, wherein the hydrogel is cross-linked.
 11. The method of claim 10, wherein the hydrogel is cross-linked with glutaraldehyde.
 12. The method of claim 10, wherein the hydrogel is cross-linked via an interpenetrating network of one or more photopolymerizable acrylates.
 13. The method of claim 8, wherein the BNP-1, BDNF, IGF-1, and Substance P are incorporated into the hydrogel.
 14. The method of claim 13, wherein the BNP-1, BDNF, IGF-1, and Substance P are incorporated into the hydrogel through covalent bonds to poly(alkylene glycol) molecules of the hydrogel.
 15. The method of claim 13, wherein the BNP-1, BDNF, IGF-1, and Substance P are incorporated into the hydrogel through entertainment within the hydrogel.
 16. The method of claim 6, wherein the matrix is a collagen gel matrix.
 17. The method of claim 16, wherein the collagen gel matrix is impregnated with the BNP-1, BDNF, IGF-1, and Substance P.
 18. The method of claim 1, wherein the BNP-1, BDNF, IGF-1, and Substance P are applied with a medium with spaced supports.
 19. The method of claim 18, wherein the spaced supports are selected from the group consisting of sponges, gels, and biopolymers. 